From 5b922bb84a9d1ac7264d665664fa7ed291ad89b1 Mon Sep 17 00:00:00 2001
From: Avani Sardana <avanisardana@MacBookAir.local>
Date: Wed, 2 Oct 2024 17:47:17 +0530
Subject: [PATCH] blogpost images
---
static/style.css | 2 +-
wiki/blogposts/aminoacids.md | 2 ++
wiki/blogposts/bradford.md | 2 ++
wiki/blogposts/cdogma_aarav.md | 8 +++-----
wiki/blogposts/cell_soham.md | 7 +++----
wiki/blogposts/cellcompetency.md | 2 ++
wiki/blogposts/clickchem.md | 18 ++++++++++++++++--
wiki/blogposts/clicknobel.md | 5 ++++-
wiki/blogposts/cloningvec.md | 2 ++
wiki/blogposts/cufreeclick.md | 3 +++
wiki/blogposts/dna.md | 2 ++
wiki/blogposts/dnarep_devansh.md | 6 +++---
wiki/blogposts/gelelectro.md | 1 +
wiki/blogposts/gene.md | 2 ++
wiki/blogposts/geneticcode.md | 3 +++
wiki/blogposts/immunostaining.md | 5 ++++-
wiki/blogposts/itc_vidhi.md | 19 ++++++-------------
wiki/blogposts/misfoldedprot.md | 2 ++
wiki/blogposts/mutations_aditey.md | 4 ++--
wiki/blogposts/ndd.md | 11 +++++++----
wiki/blogposts/neuron_ritik.md | 6 +++---
wiki/blogposts/pcr.md | 5 ++++-
wiki/blogposts/plasmids_creetika.md | 4 ++--
wiki/blogposts/proteinopathies.md | 2 ++
wiki/blogposts/rdna_mihir.md | 4 ++--
wiki/blogposts/restrictionenz.md | 3 +++
wiki/blogposts/ribosomes_vidhi.md | 4 ++--
wiki/blogposts/sdspage_soham.md | 7 +++++--
wiki/blogposts/selectablemarker.md | 2 ++
wiki/blogposts/tauopathies.md | 2 ++
wiki/blogposts/transcription.md | 4 ++--
wiki/blogposts/transformation_chandana.md | 2 ++
wiki/blogposts/translation_chandana.md | 4 ++--
wiki/blogposts/ups.md | 5 +++++
wiki/blogposts/westernblot.md | 8 ++++++--
wiki/pages/home.html | 4 +---
wiki/pages/team.html | 2 +-
37 files changed, 116 insertions(+), 58 deletions(-)
diff --git a/static/style.css b/static/style.css
index 2cd623d..67d2d54 100644
--- a/static/style.css
+++ b/static/style.css
@@ -7,7 +7,7 @@ html, body {
height: 100%;
width: 100%;
font-family: 'poppins', sans-serif;
- font-size: 16px;
+ font-size: 20px;
line-height: 1.7;
color: #222;
background-color: rgb(220, 191, 153);
diff --git a/wiki/blogposts/aminoacids.md b/wiki/blogposts/aminoacids.md
index 899a121..b631531 100644
--- a/wiki/blogposts/aminoacids.md
+++ b/wiki/blogposts/aminoacids.md
@@ -16,6 +16,8 @@ Beyond their role as residues in protein, amino acids participate in other biolo
Proteins, as said above, are polymers of amino acids. These amino acids are connected to each other by peptide bonds. Chemically, peptide bonds are an **amide linkage** formed between the carboxyl and amino groups of two amino acids.
+<img src = "https://static.igem.wiki/teams/5170/blogposts/amino-acids-and-peptide-bonds-ref-modern-biology-inc.png", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
During the process of [translation](#), peptide bonds are formed leading to the synthesis of protein. Peptide bonds also decide the overall structure of proteins. It also has broad applications in biotechnology and medicine (for example, peptide-based drugs), as peptide bonds can be synthetically created.
#### References:
diff --git a/wiki/blogposts/bradford.md b/wiki/blogposts/bradford.md
index 75dfcca..b413257 100644
--- a/wiki/blogposts/bradford.md
+++ b/wiki/blogposts/bradford.md
@@ -8,6 +8,8 @@ In any Synthetic Biology experiment which involves working with proteins, the fi
When light passes through a sample, the components of the sample absorb some of the light. Bradford's Assay is a colourimetric assay, based on **Beer-Lambert's Law** - which says that the absorbance (amount of light absorbed as a fraction of the total light incident) of a particular solution is directly proportional to the concentration of the solution.
+<img src = "https://static.igem.wiki/teams/5170/blog-images/bradford.jpeg", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
Bradford's Assay makes use of the dye CBB G-250 (Coomassie Brilliant Blue). On binding to a protein, the absorbance maximum (wavelength of light absorbed) shifts from 465nm to 595nm. This is because:
1. CBB donates free electrons to ionisable groups on protein, which disrupts the native state (the active, folded form of the protein) and exposes hydrophobic pockets
2. Hydrophobic pockets bind to the non polar region of the dye via van der Waals forces. As a consequence, positive amine groups in the protein come tête-à -tête with the negative charge of CBB.
diff --git a/wiki/blogposts/cdogma_aarav.md b/wiki/blogposts/cdogma_aarav.md
index e8b5062..0bf0d79 100644
--- a/wiki/blogposts/cdogma_aarav.md
+++ b/wiki/blogposts/cdogma_aarav.md
@@ -10,16 +10,14 @@ The **Central Dogma of Molecular Biology** is a theory which tells us the direct
[DNA](#) is the carrier of instructions (called [genetic code](#)) which are used for production of proteins useful to an organism. DNA can be replicated and distributed to daughter cells, and hence the genetic code is preserved across generations. The information flow takes place from DNA to a **[messenger RNA (mRNA)](#)** molecule, which is then used to produce the required protein molecule. This entire process is divided into two steps, **[transcription](#)** and **[translation](#).**
-Transcription is transfer of information on DNA onto a messenger molecule called mRNA.
-This is followed by translation, where the RNA delivers this information to the [ribosome](#) (part of the cell responsible for protein production). Since the mRNA plies between DNA and the ribosome, it is called a ‘messenger’. The ribosome produces the protein as per the received instructions.
+Transcription is transfer of information on DNA onto a messenger molecule called mRNA. This is followed by translation, where the RNA delivers this information to the [ribosome](#) (part of the cell responsible for protein production). Since the mRNA plies between DNA and the ribosome, it is called a ‘messenger’. The ribosome produces the protein as per the received instructions.
+
+
While most organisms follow the central dogma, there are exceptions. Baltimore and Temin theorised a process called [reverse transcription](#), in which RNA is used as a template to produce DNA (the opposite of what happens in central dogma). An example of this are **retroviruses**, which use reverse transcription to transfer their genetic information from RNA to DNA. This DNA infects the cells of the viral host, causing the cell to produce the genetic material (and proteins) of the virus.
The role of the central dogma is to define the direction in which genetic information flows. It emphasises that genetic information flows from the nucleic acids to proteins and not vice versa.
-
-
-
#### References:
Crick F, On Protein Synthesis, Symposia for the Society of Experimental Biology, (1958)
diff --git a/wiki/blogposts/cell_soham.md b/wiki/blogposts/cell_soham.md
index d38f9a8..53a0a5c 100644
--- a/wiki/blogposts/cell_soham.md
+++ b/wiki/blogposts/cell_soham.md
@@ -11,6 +11,8 @@ The cell is the basic structural[^1] and functional[^2] unit of all life forms.
Cells can be broadly categorized into prokaryotic and eukaryotic types, typically differentiated by the presence and absence of a well defined, membrane-bound nucleus[^3]. Whereas prokaryotes are unicellular[^4], eukaryotes can be unicellular as well as multicellular[^5]. Prokaryotes represent some of the first forms of life to appear on the planet.
+
+
#### Cellular Components:
1. **Cytoplasm**: Gelatinous fluid filling up a cell, containing several membrane-bound organelles.
@@ -24,13 +26,10 @@ Cells can be broadly categorized into prokaryotic and eukaryotic types, typicall
9. **Vacuoles**: Primarily store water and waste products, and may participate in controlling hydrostatic pressure[^12].
10. **Ribosome**: Large complex of protein and RNA molecules. Consist of two subunits and help in the [translation](#) process (protein synthesis). Read more about ribosomes [here](#).
- ##### (NOTE: cellular components 4-9 are present only in eukaryotes. Prokaryotes lack membrane-bound organelles)
-
+**NOTE:** cellular components 4-9 are present only in eukaryotes. Prokaryotes lack membrane-bound organelles)
**Cell Wall**: Extracellular protective cover present in certain cells. Composition differs from one cell type to the other.
-
-
#### Sources:
1. Ahmed S, Shah P, Ahmed O. Biochemistry, Lipids. [Updated 2023 May 1]. In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2024 Jan-. Available from: https://www.ncbi.nlm.nih.gov/books/NBK525952/
2. Dunn J, Grider MH. Physiology, Adenosine Triphosphate. [Updated 2023 Feb 13]. In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2024 Jan-. Available from: https://www.ncbi.nlm.nih.gov/books/NBK553175/
diff --git a/wiki/blogposts/cellcompetency.md b/wiki/blogposts/cellcompetency.md
index ac4451f..d39b011 100644
--- a/wiki/blogposts/cellcompetency.md
+++ b/wiki/blogposts/cellcompetency.md
@@ -18,6 +18,8 @@ There are various ways of making a cell competent.
Bacteria like *E.coli* when soaked in salt solutions achieve competence. Mandel and Higa in 1970 discovered that when treated with an ice cold solution of calcium chloride followed by brief heating at 37/42 °C, bacteria can be [transfected](#) with bacteriophage λ DNA. Similar methods were used for competency later on for plasmid DNA transformation in cells like *E. coli.*
Ice cold salt solutions like calcium and magnesium chloride accompanied by **heat shock** (immediate increase of temperature, which creates thermal instability and increases the permeability) are most commonly used to create small pores and this membrane permeabilisation helps in DNA uptake. The salt with divalent positively charged ions neutralise the negative charge on DNA, which reduces the repulsive forces to an extent which brings the DNA near the cell surface. Subsequenly, by heat shock, pores are created that allows the DNA to enter in the cell.
+
+<img src = "https://static.igem.wiki/teams/5170/blog-images/transduction.png", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
### Physical Methods
diff --git a/wiki/blogposts/clickchem.md b/wiki/blogposts/clickchem.md
index 1355880..58c3908 100644
--- a/wiki/blogposts/clickchem.md
+++ b/wiki/blogposts/clickchem.md
@@ -4,7 +4,7 @@ author: Devansh Jhawar
date: 29 September 2024
---
-The ‘click’ in click chemistry is intended to convey that sense of satisfaction you receive when you put Lego pieces together. In fact, the story goes that the term was coined by Jan Dueser, the wife of **K. Barry Sharpless**, the American chemist who was recently awarded the [Nobel prize](#) for his work in click reactions. Jan found the simplicity of click reactions similar to clicking Lego blocks together.
+The ‘click’ in click chemistry is intended to convey that sense of satisfaction you receive when you put Lego pieces together. In fact, the story goes that the term was coined by Jan Dueser, the wife of **K. Barry Sharpless**, the American chemist who was recently awarded the [Nobel Prize](#) for his work in click reactions. Jan found the simplicity of click reactions similar to clicking Lego blocks together.
Click reactions:
1. Have high yield and purity.
@@ -19,13 +19,27 @@ A **cycloaddition** reaction is the formation of cyclic compounds (a cyclic addu
To get to know click reactions better, let us look at the gold standard of click reactions - CuAAC and then compare it with its contemporary **Huisgen 1,3-Dipolar Cycloaddition** (non-catalysed) to understand what qualifies as a click reaction, and what does not.
-The CuACC reaction transforms an organic azide and a terminal alkyne exclusively into a triazole. A triazole consists of a five-membered ring with two carbon atoms and three nitrogen atoms. More specifically, the product is a **1,4-disubstituted 1,2,3-triazole. **
+The CuACC reaction transforms an organic azide and a terminal alkyne exclusively into a triazole. A triazole consists of a five-membered ring with two carbon atoms and three nitrogen atoms.
+
+<img src = "https://static.igem.wiki/teams/5170/blogposts/what-is-click-chemistry-2.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
+More specifically, the product is a **1,4-disubstituted 1,2,3-triazole.**
Let’s compare the non-catalysed Huisgen 1,3-dipolar cycloaddition (henceforth referred to as HDC) with the copper-catalyzed variant, CuAAC - to understand why one is a click reaction and the other isn’t.
+<img src = "https://static.igem.wiki/teams/5170/blogposts/what-is-click-chemistry-1.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
1. Right off the bat, HDC forms two isomers, whereas CuACC yields a single product. A click reaction is highly specific and yields a high-purity product with no other byproducts. The formation of a single product eliminates the need for further purification in the case of CuACC.
2. HDC requires high temperatures (sometimes above 100°C) to proceed. These conditions limit the reaction’s applicability with heat-sensitive substrates. CuACC occurs under mild conditions like room temperature, which increases the sensitivity of the reaction to certain other molecules.
3. Talking about sensitivity, the CuACC has a wide range of tolerance for functional groups. For example, the presence of carboxyl, amino, hydroxyl, etc. functional groups does not interfere with the reaction, making it a lot more versatile than HDC.
3. The uncatalysed reaction is slow, often taking hours or even days to achieve completion, whereas CuACC is extremely fast and essentially irreversible, and is usually complete within minutes.
Basically, click reactions are just better, and all other reactions have a skill issue when compared with click reactions.
+
+#### References:
+1. Zihau Xu, Kaitlin M. Bratlie. (2018, May 26). Click Chemistry and Material Selection for in Situ Fabrication of Hydrogels in Tissue Engineering Applications. ACS Publications.
+2. Lisa M. Gaetke, Ching Kuang Chow *Copper toxicity, oxidative stress, and antioxidant nutrients*
+3. Jeremy M. Baskin; Jennifer A. Prescher; Scott T. Laughlin; Nicholas J. Agard; Pamela V. Chang; Isaac A. Miller; Anderson Lo; Julian A. Codelli; Carolyn R. Bertozzi (2007). *"Copper-free click chemistry for dynamic in vivo imaging".* Proceedings of the National Academy of Sciences.
+4. Rostovtsev, VV, Green, LG, Fokin, VV, Sharpless, KB. (2002) *Angew. Chem..* 114, 2596.
+5. Olof Ramstrom. (2022, October 5). Scientific Background on the Nobel Prize in Chemistry 2022, CLICK CHEMISTRY AND BIOORTHOGONAL CHEMISTRY. The Nobel Committee for Chemistry
+6. Images: Future Journal of Pharmaceutical Sciences
diff --git a/wiki/blogposts/clicknobel.md b/wiki/blogposts/clicknobel.md
index 4d7a458..f5246e4 100644
--- a/wiki/blogposts/clicknobel.md
+++ b/wiki/blogposts/clicknobel.md
@@ -8,9 +8,12 @@ Picture this: it's the 1990s. Scientists are trying to figure out a way to make
However, the reaction itself was difficult to achieve. The rates were low at ambient temperature (which is undesirable), and azides are often explosive in nature, which discouraged industrial companies to produce it. This changed when **Morten Meldal** and **Christian W. Tornoe** discovered that active copper-species can be used as a catalyst, which increased the reaction rate by upto 10^7 times!
+<img src = "https://static.igem.wiki/teams/5170/blogposts/why-click-chemistry-won-the-nobel-ref-american-chemical-society.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
Copper is a toxic substance for human beings, and hence another hurdle arose for cycloaddition click reaction to be carried out in human beings. Enter **Carolyn R. Bertozzi**, who devised a new way to initiate it - SPAAC (strain-promoted azide-alkyne cycloaddition), that is, [copper free click chemistry](#). Bertozzi and her team showed that SPAAC reaction involving a substituted cyclooctyne structure (cyclooctyne, by itself, is heavily strained) and azides proceeded as expected (without the use of copper). Now, the reaction has been fine-tuned to be used in living creatures.
The joint effort of all these people created something which can very much be [used](#) by human beings and improve their lives, which fetched them the **Nobel Prize in Chemistry** in 2022.
#### References:
-1. Olof Ramstrom. (2022, October 5). Scientific Background on the Nobel Prize in Chemistry 2022, CLICK CHEMISTRY AND BIOORTHOGONAL CHEMISTRY. The Nobel Committee for Chemistry
\ No newline at end of file
+1. Olof Ramstrom. (2022, October 5). Scientific Background on the Nobel Prize in Chemistry 2022, CLICK CHEMISTRY AND BIOORTHOGONAL CHEMISTRY. The Nobel Committee for Chemistry
+2. Image: American Chemical Society
\ No newline at end of file
diff --git a/wiki/blogposts/cloningvec.md b/wiki/blogposts/cloningvec.md
index e33bade..9e49f52 100644
--- a/wiki/blogposts/cloningvec.md
+++ b/wiki/blogposts/cloningvec.md
@@ -8,6 +8,8 @@ A **cloning vector** is like a transportation vehicle. It helps to put foreign [
In 1973, Cohen and Boyer made a significant breakthrough by developing the first cloning vector, a [plasmid](#) (aA DNA molecule generally present in bacteria that can replicate independently of the genomic DNA).
+
+
First, a fragment of DNA from a foreign microbe is cut using a [restriction enzyme](#). The foreign DNA fragment is then joined with the vector DNA through the process of [molecular ligation](#), often using the enzyme DNA ligase. The **recombinant vector** (foreign DNA + vector DNA) is then introduced into the host cell. If the host cell accepts the recombinant DNA, the replication process of DNA starts producing multiple clones of the foreign DNA with itself. The cells that successfully performed cloning are screened and separated from the group.
A cloning vector has some key features:
diff --git a/wiki/blogposts/cufreeclick.md b/wiki/blogposts/cufreeclick.md
index a1e58bc..3fce172 100644
--- a/wiki/blogposts/cufreeclick.md
+++ b/wiki/blogposts/cufreeclick.md
@@ -15,6 +15,8 @@ Copper free [click chemistry](#) encompasses [bioorthogonal reactions](#) that d
It is based on Wittig's copper free click reaction. It is a reaction between cyclooctyne and phenyl azide to produce a single product, a triazole, in an extremely fast reaction. The reaction moves forward due to the **ring strain** in the cyclooctyne. Ring strain refers to the instability arising due to differences in bond angles. The ideal bond angle for an alkyne is 180 degree, but cyclooctyne has an angle of 160 degree, which causes strain. Other derivatives of cyclooctyne that are used for copper free chemistry are OCT, MOFO (monofluorinated cyclooctyne), DIFO (difluorinated cyclooctyne) and MFCO (monofluorosubstituted cyclooctyne).
+<img src = "https://static.igem.wiki/teams/5170/blogposts/copper-free-click-chemistry-ref-sigmaaldrich.png", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
### Applications
Copper free click chemistry is used for labeling biomolecules in *live laboratory mice*. Mice are the model organism for understanding human biological systems due the similarities in their biology. It was successfully used to label molecules called azidosugars without any damage to tissues like intestines, heart and liver of the mice, due to copper toxicity. Particularly, copper free click chemistry presents a good option for facilitating clicking in Alzheimer's prone or Alzheimer's afflicted systems.
@@ -24,3 +26,4 @@ Copper free click chemistry is used for labeling biomolecules in *live laborator
3. Jeremy M. Baskin; Jennifer A. Prescher; Scott T. Laughlin; Nicholas J. Agard; Pamela V. Chang; Isaac A. Miller; Anderson Lo; Julian A. Codelli; Carolyn R. Bertozzi (2007). *"Copper-free click chemistry for dynamic in vivo imaging".* Proceedings of the National Academy of Sciences.
4. Rostovtsev, VV, Green, LG, Fokin, VV, Sharpless, KB. (2002) *Angew. Chem..* 114, 2596.
5. Akeroyd N. (2010) *Click chemistry for the preparation of advanced macromolecular architectures* Stellenbosch University.
+6. Image: Sigma Aldrich
diff --git a/wiki/blogposts/dna.md b/wiki/blogposts/dna.md
index f668e0b..8577f8e 100644
--- a/wiki/blogposts/dna.md
+++ b/wiki/blogposts/dna.md
@@ -16,6 +16,8 @@ The nucleotides are joined together by covalent bonds called **phosphodiester li
In 1953, James Watson and Francis Crick proposed the famous double helix model based on X-ray diffraction data obtained by Rosalind Franklin and Maurice Wilkins. DNA does not usually exist as single strand or chain but instead as a pair of strands that are tightly held together. These two long strands coil around each other in the shape of a double helix.
+<img src = "https://static.igem.wiki/teams/5170/blog-images/dna.png", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
The DNA double helix is stabilised primarily by two forces -- hydrogen bonds between nucleotides and base stacking interactions among aromatic nucleobases. The two strands are complementary to each other because hydrogen bonds are formed between specific bases only - adenine with thymine, and cytosine with guanine. Both strands of DNA store the same biological information. The DNA chain measures 2.2-2.6nm wide, and one nucleotide unit measures 0.33nm long.
A large part of DNA (more than 98%) in human is [non-coding](#), meaning that these sections do not serve as patterns for protein synthesis. The genetic information carried by DNA is held in sequences of pieces of DNA called [genes](#). These genes regulate protein synthesis resulting in traits of organisms.
diff --git a/wiki/blogposts/dnarep_devansh.md b/wiki/blogposts/dnarep_devansh.md
index 62fc5f3..2e4f88c 100644
--- a/wiki/blogposts/dnarep_devansh.md
+++ b/wiki/blogposts/dnarep_devansh.md
@@ -11,18 +11,18 @@ Since DNA is a double stranded helix, the process is initiated by the enzyme **h
The precision of the enzymes that synthesise new DNA strands is extremely high, since errors in DNA replication can result in [mutations](#), which may be harmful for the organism. By the time the replication is complete, we have two identical DNA molecules, each containing one old strand and a newly synthesised one – thus making the process **semi-conservative.**
+
+
A quote from Watson and Crick's landmark 1953 paper suggests the motivation behind this discovery:
<p align = "center">
-_"It has not escaped our notice that the specific pairing we have postulated immediately suggests a possible copying mechanisms for the genetic material."_
+*"It has not escaped our notice that the specific pairing we have postulated immediately suggests a possible copying mechanisms for the genetic material."*
</p>
DNA replication can also be performed artificially, outside the cell. One such way of doing this is by **[Polymerase Chain Reaction (PCR)](#)**. This is useful when you have a limited amount of DNA sample and need to analyse or use it further.
-
-
#### References:
1. Crick, F. H. S. Codon-anticodon pairing: The wobble hypothesis. Journal of Molecular Biology 19, 548-555 (1966)
2. Johnson, R. E., et al. Fidelity of human DNA polymerase $\eta$. Journal of Biological Chemistry 275, 7447-7450 (2000)
diff --git a/wiki/blogposts/gelelectro.md b/wiki/blogposts/gelelectro.md
index d36be4d..4279162 100644
--- a/wiki/blogposts/gelelectro.md
+++ b/wiki/blogposts/gelelectro.md
@@ -20,4 +20,5 @@ Agarose Gel Electrophoresis has many applications ranging from separation of DNA
1. Jeppsson JO, Laurell CB, Franzén B, Agarose Gel Electrophoresis, Clinical Chemistry, (1979)
2. Lee PY, Costumbrado J, Hsu CY, Kim YH, Agarose gel electrophoresis for the separation of DNA fragments, Journal of Visualized Experiments (2012).
+3. Image: TechnologyNetworks
diff --git a/wiki/blogposts/gene.md b/wiki/blogposts/gene.md
index c5fc183..1e7772b 100644
--- a/wiki/blogposts/gene.md
+++ b/wiki/blogposts/gene.md
@@ -6,6 +6,8 @@ date: 2 October 2024
The term ‘gene’ is defined variedly throughout different aspects of biology. It is vaguely defined as there is no particular definition for a gene. The two major definitions widely used are the Mendelian gene and the molecular gene. Mendelian gene is defined as the **basic unit of heredity,** that is, the passing on of characters from one generation to the next. On the other hand, the **molecular gene** is defined as a sequence of nucleotides in DNA that is transcribed to produce a functional RNA.
+<img src = "https://static.igem.wiki/teams/5170/blog-images/gene.png", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
In the 1860s, Gregor Mendel suggested the existence of discrete inheritable units. The term ‘gene’ was introduced by Wilhelm Johannsem in 1909. It originates from the Greek word ‘gonos’ which means offspring and procreation. Our modern understanding of genes has so far come to as ‘a functional unit of DNA’.
In [DNA](#), there are two types of genes:
diff --git a/wiki/blogposts/geneticcode.md b/wiki/blogposts/geneticcode.md
index e79d56c..fab5c6b 100644
--- a/wiki/blogposts/geneticcode.md
+++ b/wiki/blogposts/geneticcode.md
@@ -14,7 +14,10 @@ The genetic code is said to be **degenerate**, because a single amino acid can b
The genetic code, outlining which codon corresponds to which amino acid, is given below.
+<img src = "https://static.igem.wiki/teams/5170/blogposts/genetic-code-ref-openoregon.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
#### References:
1. James D Watson, Tania Baker, Stephen Bell, Alexander Gann, Michael Levine, Richard Losick, Molecular Biology of the Gene, India: Affiliated East West Press, 2024
2. Koji Tamura. (2016, Aug 25). The Genetic Code: Francis Crick’s Legacy and Beyond. National Library of Medicine.
+3. Image: OpenOregon
diff --git a/wiki/blogposts/immunostaining.md b/wiki/blogposts/immunostaining.md
index b3289af..13cdbb0 100644
--- a/wiki/blogposts/immunostaining.md
+++ b/wiki/blogposts/immunostaining.md
@@ -12,13 +12,15 @@ The antigen has small sites on it which bind to the receptors of the antibodies
The same principle of antigen-antibody interaction is used in immunostaining, except that here the antibodies are introduced into the sample externally (and not produced by the body). They bind to the target antigen only.
The antibodies used in this process are linked to an enzyme or fluorophore. The conjugated enzymes are reacted further with a substrate, eventually forming a coloured or chemiluminescent product. Fluorophores are chemicals that absorb and emit energy in a predictable fashion. This eventually makes the antibodies easy to spot under the microscope. Pathologists interpret the slide and determine whether a target antigen is present or absent thus completing the diagnosis.
+
+<img src = "https://static.igem.wiki/teams/5170/blogposts/immunostaining-ref-bd-biosciences.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
Immunostaining has emerged as a commonly used and valuable technique in diagnosis. However, some disadvantages are associated with the application of this technique. Immunostaining encompasses a few different methods:
1. **Immunohistochemistry:** the antibodies bound to the antigens are stained with dyes or enzymes and this is placed on a glass slide that is evaluated under the microscope.
2. **Flow cytometry:** the antibodies are stained, and a laser is used to analyses the sample and sort all the cells on by one into different categories.
3. **Immuno-electron microscopy:** antibodies are linked to nanoparticles of gold. Gold is visible as dark flecks under an electron microscope; thus, it is easy to examine the sample.
-Immunostaining methods are extensively used in **protein Purification,** that is, a the process of separation of certain target protein from a mixture of other molecules/cells/tissues or whole organisms. Protein purification is a highly researched field as the process is often crucial in diagnosis of infections.
+Immunostaining methods are extensively used in **protein purification,** that is, a the process of separation of certain target protein from a mixture of other molecules/cells/tissues or whole organisms. Protein purification is a highly researched field as the process is often crucial in diagnosis of infections.
Immunostaining can be used to investigate the presence or absence of a certain protein, its distribution in a tissue and across regions and parts of a cell. Once the different proteins in a sample have been separated by [SDS-PAGE](#) and [Western Blotting](#), the band corresponding to the protein is often identified using immunostaining. Antibodies against the protein of interest, conjugated with an enzyme or fluorophore (as before), are used for this purpose.
@@ -26,6 +28,7 @@ Immunostaining can be used to investigate the presence or absence of a certain p
1. Idleburg, C., Lorenz, M. R., DeLassus, E. N., Scheller, E. L., & Veis, D. J. (2021). Immunostaining of Skeletal Tissues. Methods in molecular biology (Clifton, N.J.), 2221, 261–273.
2. Binch, A., Snuggs, J., & Le Maitre, C. L. (2020). Immunohistochemical analysis of protein expression in formalin fixed paraffin embedded human intervertebral disc tissues. JOR spine, 3(3), e1098.
3. Maity, B., Sheff, D., & Fisher, R. A. (2013). Immunostaining: detection of signaling protein location in tissues, cells and subcellular compartments. Methods in cell biology, 113, 81–105.
+4. Image: BD Biosciences
diff --git a/wiki/blogposts/itc_vidhi.md b/wiki/blogposts/itc_vidhi.md
index f7dc930..14de8e2 100644
--- a/wiki/blogposts/itc_vidhi.md
+++ b/wiki/blogposts/itc_vidhi.md
@@ -6,27 +6,19 @@ date: 7 September 2024
<p align = "center">
-Isothermal Titration Calorimetry is often considered the gold standard for studying interactions between molecules, primarily because of its capability to measure thermodynamic and kinetic quantities with one experiment.
+*Isothermal Titration Calorimetry is often considered the gold standard for studying interactions between molecules, primarily because of its capability to measure thermodynamic and kinetic quantities with one experiment.*
</p>
Isothermal Titration Calorimetry (ITC) is an experimental procedure used to calculate the heat of a reaction at different concentrations of the reactants. One reactant is added gradually to a solution containing the other reactants. The reaction occurs, and a device called a **calorimeter** monitors the heat released or absorbed due to this addition.
-The **heat of a reaction** is defined as the amount of heat that must be added or deducted from the reaction system to maintain the reactants at a constant temperature. When the reaction is performed at a constant pressure, this heat represents a thermodynamic quantity called **enthalpy of the reaction** (ΔH).
+The **heat of a reaction** is defined as the amount of heat that must be added or deducted from the reaction system to maintain the reactants at a constant temperature. When the reaction is performed at a constant pressure, this heat represents a thermodynamic quantity called **enthalpy of the reaction** (ΔH). This information can be used to determine the **binding affinity of the reaction** (the tendency of the reactants to react and form chemical bonds with each other), the **binding stoichiometry** (ratio of reactants binding with each other in the reaction) and **molar enthalpy change** (enthalpy of reaction per mole of the reactants reacting with each other). These in turn can be used to calculate other thermodynamic quantities like the **Gibbs Free Energy change** (ΔG, a measure of the spontaneity of a certain reaction) and the **entropy change** (ΔS, the measure of randomness of a system).
-This information can be used to determine the **binding affinity of the reaction** (the tendency of the reactants to react and form chemical bonds with each other), the **binding stoichiometry** (ratio of reactants binding with each other in the reaction) and **molar enthalpy change** (enthalpy of reaction per mole of the reactants reacting with each other).
+The experimental setup consists of two **titration cells** – one is a control cell and contains only a **buffer solution**, while the other is an **experimental cell** containing the buffer and some (but not all) of the reactants. A buffer solution is a solution whose pH remains constant despite the addition of an acid, base or water. Both of these cells are placed in an **adiabatic** jacket – this means that no heat transfer is possible between the reaction system and the surrounding environment. **Thermopiles** made of semiconductor material measure the temperature differences between the control cell and the experimental cell. A heat sink equalises the temperature difference caused by the reaction. The thermopiles generate a potential difference proportional to the difference in temperature at their two junctions. In this case, this is the difference between the control and experimental cells.
-These in turn can be used to calculate other thermodynamic quantities like the **Gibbs Free Energy change** (ΔG, a measure of the spontaneity of a certain reaction) and the **entropy change** (ΔS, the measure of randomness of a system).
+<img src = "https://static.igem.wiki/teams/5170/blogposts/itc-reference-physiological-chemistry-lmu-munich.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "itc">
-The experimental setup consists of two **titration cells** – one is a control cell and contains only a **buffer solution**, while the other is an **experimental cell** containing the buffer and some (but not all) of the reactants. A buffer solution is a solution whose pH remains constant despite the addition of an acid, base or water.
-
-Both of these cells are placed in an **adiabatic** jacket – this means that no heat transfer is possible between the reaction system and the surrounding environment. **Thermopiles** made of semiconductor material measure the temperature differences between the control cell and the experimental cell. A heat sink equalises the temperature difference caused by the reaction.
-
-The thermopiles generate a potential difference proportional to the difference in temperature at their two junctions. In this case, this is the difference between the control and experimental cells.
-
-The reactant not already present in the experimental cell is then titrated - that is, added slowly in very small amounts – to both the cells. Heat changes occur due to dilution, the addition of reactant, as well as the reaction itself. This causes a temperature difference, which is detected by the thermopiles and converted into a potential difference.
-
-This difference is proportional to the power at which the heat sink works to transfer heat to or from the experimental cell. The power spike required to equalise the temperatures is recorded with time. This is called a **thermogram**. The area under each spike is added up and plotted against the molar ratio of the titrant (reactant added to the solution during titration). All the quantities mentioned at the beginning of the article can be determined using this graph.
+The reactant not already present in the experimental cell is then titrated - that is, added slowly in very small amounts – to both the cells. Heat changes occur due to dilution, the addition of reactant, as well as the reaction itself. This causes a temperature difference, which is detected by the thermopiles and converted into a potential difference. This difference is proportional to the power at which the heat sink works to transfer heat to or from the experimental cell. The power spike required to equalise the temperatures is recorded with time. This is called a **thermogram**. The area under each spike is added up and plotted against the molar ratio of the titrant (reactant added to the solution during titration). All the quantities mentioned at the beginning of the article can be determined using this graph.
This remarkable process is used for interactions between proteins and DNA, studying reactions of enzymes and analysing various drugs. Truly, it is an indispensable procedure in experimental chemistry as well as biology.
@@ -36,3 +28,4 @@ This remarkable process is used for interactions between proteins and DNA, study
2. Margarida Bastos, Olga Abian, Christopher M. Johnson, Frederico Ferreira-da-Silva, Sonia Vega, Ana Jimenez-Alesanco, David Ortega-Alarcon & Adrian Velazquez-Campoy (2023, March 9). *Isothermal titration calorimetry*. Nature Reviews Methods Primers.
3. Margarida Bastos & Adrian Velazquez-Campoy (2021, March 4). *Isothermal titration calorimetry (ITC): a standard operating procedure (SOP)*. Springer Link.
4. Johnston, H.D.,The thermodynamics (log K, ΔH°, ΔS°, ΔCp°) of metal ligand interaction in aqueous solution (PhD). *Brigham Young University ScholarsArchive* (1968).
+5. Image: Physiological Chemistry LMU Munich
diff --git a/wiki/blogposts/misfoldedprot.md b/wiki/blogposts/misfoldedprot.md
index 748baff..462977e 100644
--- a/wiki/blogposts/misfoldedprot.md
+++ b/wiki/blogposts/misfoldedprot.md
@@ -13,6 +13,8 @@ This is known as the secondary structure of the protein.
These secondary structures then fold to form compact functional structures. Depending on the function they have to perform, they assume a specific 3D structure. It is this **tertiary structure** that determines the biological function of the protein. The specific shape allows the protein to interact with other molecules, perform catalytic functions, or provide structural support. It is also important to understand that a **misfolding** resulting in an erroneous tertiary structure can lead to many diseases.
+<img src = "https://static.igem.wiki/teams/5170/blogposts/export202407280116098149.png", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
Protein-folding research began before we knew about diseases caused by protein misfolding. Before 1972, it was believed that infectious diseases were caused by viruses and bacteria. Stanley Prusiner’s research on Creutzfeldt-Jakob disease revealed that misfolded proteins, known as **prions**, could also be responsible for disease. This discovery changed our understanding of many conditions, showing that protein misfolding is also involved in diseases like Alzheimer’s, Parkinson’s, Huntington’s, and type II diabetes.
What's amazing is that proteins can self-assemble spontaneously and reversibly into their unique native three-dimensional structure under suitable physiological conditions. Here, “spontaneous†means that no external energy source such as ATP hydrolysis is required. This led scientists to believe that it was the amino acid sequence that dictated the way that the protein would fold. In other words, all the information required for a protein to adopt the correct three-dimensional conformation is provided by its amino acid sequence!
diff --git a/wiki/blogposts/mutations_aditey.md b/wiki/blogposts/mutations_aditey.md
index 4f32af2..e69a055 100644
--- a/wiki/blogposts/mutations_aditey.md
+++ b/wiki/blogposts/mutations_aditey.md
@@ -40,6 +40,8 @@ Example: (the |xyz| represent one codon:)
Broadly speaking, since a mutation is an ‘error in DNA copying,’ it occurs when the replication mechanism breaks down or makes errors. There are systems in place to correct the mistakes made by a process called DNA repair,, but sometimes they escape it.
+
+
Several factors, called mutagens, exacerbate the rate of mutations:
1. **Radiations:** X-Rays, Gamma Rays, and other high energy radiations can cause breaks in DNA strands, leading to large scale mutations which can cause cancer (and unfortunately won’t make you the Hulk).
2. **Biological Agents:** Some viruses, upon infection, can interfere with the genetic material, potentially leading to mutations.
@@ -48,8 +50,6 @@ Several factors, called mutagens, exacerbate the rate of mutations:
Most mutations are neutral and have no significant impact on the body, however some mutations do have effects. These may be beneficial – some mutations in bacteria help them develop antibiotic resistance. Some mutations can be extremely harmful, and can cause diseases like cancer or genetic disorders like cystic fibrosis and Huntington’s disease.
Mutations are critical for evolution and are the primary source for genetic variation. These variations allow organisms to adapt in a changing environment. However, mutations are not always beneficial and can lead to various disorders. Understanding mutations is key to advances in medical sciences. There is also work being done to manipulate these mutations.
-
-
 
#### References:
diff --git a/wiki/blogposts/ndd.md b/wiki/blogposts/ndd.md
index 5a9e695..1b1cb77 100644
--- a/wiki/blogposts/ndd.md
+++ b/wiki/blogposts/ndd.md
@@ -10,6 +10,8 @@ Regeneration is one of nature’s most captivating feats. 
It's a testament to the resilience and adaptability of life. A planarian worm (eg. *Taenia solium* (pork tapeworm)), can be cut into many pieces and each piece will regrow into a full worm within about two weeks. Although the regenerative capacity in human beings is limited, it plays a significant role in our everyday lives.
+<img src = "https://static.igem.wiki/teams/5170/blogposts/brain-reference-maropeng-visitor-center.png", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
Ironically, the most important and intricate cells of our body, the nerve cells or [neurons](#) have very limited regenerative capacity. **Neuroregeneration** is defined as the regrowth or repair of nervous tissues,cells or cell products. Neuroregenerative mechanisms may include generation of new neurons, glia, axons, myelin, or synapses. Neuroregeneration differs between the peripheral nervous system (PNS) and the central nervous system (CNS) (that is, the brain and spinal cord) with regards to the functional mechanisms involved, especially in the extent and speed of repair. Unlike a peripheral nervous system (everything apart from the brain and spinal cord) injury, injury to the central nervous system is not followed by extensive regeneration.
**Neurodegeneration** is defined as a complex process that causes death of neurons in the brain and spinal cord, resulting in damage and dysfunction. Chronic neurodegeneration leads to **neurodegenerative diseases**, a condition that damages and destroys parts of our nervous system over time, especially our brain. These conditions are permanent and incurable.
@@ -34,17 +36,17 @@ The symptoms of neurodegenerative diseases can vary widely, even among people wi
Alzheimer's disease is alarmingly prevalent and has a significant impact globally.Over 55 million people worldwide are living with dementia and Alzheimer's disease contributes to 60-70% of these cases. Alzheimer's disease is a significant cause of morbidity and mortality among the elderly in India.  While exact statistics on Alzheimer's as a cause of death can vary, it is known to be one of the  leading causes of dementia, which affects over 1 million individuals in the country.
-# Symptoms
+#### Symptoms
The most common early symptom is difficulty in remembering recent events. As the disease advances, symptoms can include  problems with language, disorientation (including easily getting lost), mood swings, loss of motivation,self-neglect, and behavioral issues. As a person's condition declines, they often withdraw from family and society. Gradually, bodily functions are lost, ultimately leading to death. Although the speed of progression can vary, the average life expectancy following diagnosis is three to twelve years.
-# Causes
+#### Causes
The cause for most Alzheimer's cases is still mostly unknown, except for 1–2% of cases where deterministic genetic differences have been identified. Several competing hypotheses attempt to explain the underlying cause; the most predominant hypothesis is the **amyloid beta (Aβ) hypothesis.**
When abnormal amounts of amyloid beta (Aβ) protein accumulate extracellularly as **amyloid plaques and tau proteins**, or inside the cell as neurofibrillary tangles in the brain, it affects our brain's neuronal functioning and connectivity, resulting in a progressive loss of brain function. This altered protein clearance ability is age-related, regulated by brain cholesterol, and associated with other neurodegenerative diseases.
-# Pathophysiology
+#### Pathophysiology
Alzheimer's disease is characterized by loss of neurons and synapses in the cerebral cortex and certain subcortical regions. This loss results in gross wasting away of the affected regions, including degeneration in the temporal lobe and parietal lobe, and parts of the frontal cortex and cingulate gyrus.
@@ -66,4 +68,5 @@ The ABC score put together classifies the neuropathological changes by the disea
1. Lamptey RN, Chaulagain B, Trivedi R, Gothwal A, Layek B, Singh J; A Review of the Common Neurodegenerative Disorders: Current Therapeutic Approaches and the Potential Role of Nanotherapeutics; Int J Mol Sci; February 2022
2. Patow, Gustavo; Escrichs, Anira; Ritter, Petra; Deco, Gustavo; Whole-Brain Dynamics Disruptions in the Progression of Alzheimer's Disease: Understanding the Influence of Amyloid-Beta and Tau"; bioRxiv; March 2024
-3. Erkkinen, Michael G.; Kim, Mee-Ohk; Geschwind, Michael D. Clinical Neurology and Epidemiology of the Major Neurodegenerative Diseases. Cold Spring Harbor Perspectives in Biology. April 2018
\ No newline at end of file
+3. Erkkinen, Michael G.; Kim, Mee-Ohk; Geschwind, Michael D. Clinical Neurology and Epidemiology of the Major Neurodegenerative Diseases. Cold Spring Harbor Perspectives in Biology. April 2018
+4. Image: Maropeng Visitor Center
\ No newline at end of file
diff --git a/wiki/blogposts/neuron_ritik.md b/wiki/blogposts/neuron_ritik.md
index 087ee54..fbc927f 100644
--- a/wiki/blogposts/neuron_ritik.md
+++ b/wiki/blogposts/neuron_ritik.md
@@ -6,7 +6,7 @@ date: 7 September 2024
---
<p align = "center">
-_"It is the little grey cells, mon ami, on which one must rely."_
+*"It is the little grey cells, mon ami, on which one must rely."*
</p>
@@ -22,14 +22,14 @@ The neuron consists of a **cell body** or soma which houses the [nucleus](#) of
The way the neuron fires is through a longer process from the cell body known as the **axon**. The axon is primarily responsible for the transmission of impulses away from the neuron towards the dendrites of other neurons. They can be really long, sometimes even around a meter in length! Axons sometimes have a discontinuous layer of insulating fat known as the **myelin sheath.** Gaps in the myelin sheath are called **Nodes of Ranvier.** This helps in increasing the speed of transmission of the nerve impulses, as impulses jump from node to node instead of traversing the whole distance.
+
+
Impulses travel through a neuron using electrical signals. These signals arise from a difference in charge created by ion channels, which act as "invite only highways" for sodium and potassium ions. This charge difference is manifested as a change in potential difference across the neuron membrane – called an **action potential,** the impulse that moves along the axon.
This still doesn’t explain how neurons communicate with each other. Our nerves employ usage of specialised chemicals called **neurotransmitters** - the FedEx of our nervous system! These transmit the signal through a gap between neurons called a **synapse,** and cause excitation or inhibition of the next neuron. Axon terminals are the endpoints of the axon where neurotransmitters are released.
Neurotransmitters (and other important compounds) are synthesised in the cell body, by clusters of [ribosomes](#) (protein factories) called **Nissl’s Granules.**
-
-
#### References:
1. Ackerman, S. (1992). Discovering the brain. National Academies Press
diff --git a/wiki/blogposts/pcr.md b/wiki/blogposts/pcr.md
index 3388dd5..e87d260 100644
--- a/wiki/blogposts/pcr.md
+++ b/wiki/blogposts/pcr.md
@@ -15,9 +15,12 @@ A single PCR cycle involves the following steps:
2. **Annealing:** The strands are cooled down to 48-72°C. This allows primer molecules present in the reaction mixture to bind with them.
3. **Extension:** DNA polymerase adds complementary nucleotides to the single strands of DNA. Thus, two copies of DNA are obtained at the end of the cycle.
+<img src = "https://static.igem.wiki/teams/5170/blogposts/pcr-ref-britannica.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
With each cycle, the number of DNA copies doubles – that is, it exponentially increases (2n after n cycles). One cycle takes around three minutes. Thus, a billion gene replicas can be produced in a few hours. After amplification, the DNA obtained is purified and then used for other processes.
Fun fact: PCR uses a special type of polymerase called Taq polymerase which is functional even at the high temperatures of the thermal cycler (while normal human enzymes would get denatured). It is isolated from the bacterium *Thermus aquaticus*.
#### References:
-1. Khehra N, Padda IS, Swift CJ. Polymerase Chain Reaction (PCR) [Updated 2023 Mar 6]. Treasure Island (FL): StatPearls Publishing; 2024 Jan-.
\ No newline at end of file
+1. Khehra N, Padda IS, Swift CJ. Polymerase Chain Reaction (PCR) [Updated 2023 Mar 6]. Treasure Island (FL): StatPearls Publishing; 2024 Jan-.
+2. Image: Britannica
\ No newline at end of file
diff --git a/wiki/blogposts/plasmids_creetika.md b/wiki/blogposts/plasmids_creetika.md
index 435c77f..f7ce977 100644
--- a/wiki/blogposts/plasmids_creetika.md
+++ b/wiki/blogposts/plasmids_creetika.md
@@ -7,14 +7,14 @@ date: 7 September 2024
Plasmids are **extrachromosomal** [DNA](#) (apart from the main genetic material) present as circular structures in cells. They contain "accessory" [genes](#) that express specific proteins. In bacteria, these genes may code for antibiotic resistance, [enzymes](#) to utilise unique nutrient sources, virulence (the ability to cause disease), degradation of toxic compounds, and much more. Think about plasmids in cells as accessory apps on your phone: while an antivirus is not strictly required for the phone to function, it is definitely beneficial.
+
+
Plasmids mobilise these genes via horizontal transfer; that is, by methods other than traditional reproduction. This includes **conjugation** (cell-cell contact), **transduction** (bacteriophage, a virus which infects bacteria, carries the DNA and infects another bacterium), and **[transformation](#)** (uptake of free plasmid DNA by organisms), among others.
Interestingly, one cell contains many copies of the same plasmid, which in turn contains all the gene products necessary for its own survival. Additionally, plasmids can sometimes be detrimental to cells when their proteins are environmentally unfavorable. This has led to the plasmid paradox; should cells with plasmids really be more preferred by selection? Either way, the potential for plasmid study and research are exciting.
In the lab, plasmids are used as **[vectors](#)** for [gene cloning](#). First, circular DNA is cut with a [restriction enzyme](#) to produce linear DNA. The genes to be cloned are introduced to the cut plasmid and covalently joined using **DNA ligase**. Finally, this modified recombinant DNA is reintroduced into bacterial cells (transformation), where large amounts of their corresponding protein is produced. This is a fundamental process in [genetic engineering](#).
-
-
#### References:
1. Alberts, Bruce, et al. Molecular Biology of the Cell. 6th ed., Garland Science, 2014.
diff --git a/wiki/blogposts/proteinopathies.md b/wiki/blogposts/proteinopathies.md
index 0c181f7..a3d2a41 100644
--- a/wiki/blogposts/proteinopathies.md
+++ b/wiki/blogposts/proteinopathies.md
@@ -6,6 +6,8 @@ date: 1 October 2024
[Neurodegenerative diseases (NDDs)](#) are characterised by progressive deterioration of parts of the nervous system, such as the neurons, their synapses or glial cells. In some NDDs, this may be caused by deposition of proteins in the nervous system. In particular, when a protein misfolding leads to its deposition, it is called a **proteinopathy.**
+<img src = "https://static.igem.wiki/teams/5170/blogposts/export202407280116098149.png", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
Since proteins are long polymers, they form characteristic three dimensional structures in order to remain compact. This is known as [protein folding](#). Generally, a protein will spontaneously fold into a structure that is the least energetic thermodynamically. This particular structure allows parts of the protein to interact with other molecules and receptors in the cell.
However, in certain cases, there may be two structures that are vastly different structurally, but have comparable energies. While one structure is the native one in the body and has a particular function, the other may be useless or even toxic. The body has developed molecules known as **‘chaperones’**, which bind to the proteins and allow them to fold only in the correct structure by inhibiting the pathway that forms alternative, unwanted structure. However, given the large number of proteins present in the body, some still misfold due to random chance and form linear or fibrillar aggregates known as amyloid deposits.
diff --git a/wiki/blogposts/rdna_mihir.md b/wiki/blogposts/rdna_mihir.md
index 4d2f372..b2c5cd2 100644
--- a/wiki/blogposts/rdna_mihir.md
+++ b/wiki/blogposts/rdna_mihir.md
@@ -9,6 +9,8 @@ Recombinant DNA, sometimes denoted as rDNA, is a [DNA](#) strand artificially cr
In 1972, Paul Berg was trying to understand how genes from different organisms function together. His experiments laid the foundations for recombinant DNA. He showed that DNA from different organisms can be joined together to make something new. Paul Berg is widely known today as the ‘Father of Recombinant DNA Technology’. Just a year later, in 1973, Herbert Boyer and Stanley Cohen successfully inserted a gene from an African clawed frog into bacterial DNA, thus proving that DNA cloning is feasible.
+
+
But, why is rDNA so important? It has a wide range of applications, some of which are listed below:
1. **Health:**
@@ -27,8 +29,6 @@ a. **[Gene Cloning](#)** - Researchers use the rDNA technology to clone (essenti
These applications of rDNA technology highlight its immense potential and versatility. As we continue to explore its possibilities, the future of medicine, agriculture, and scientific research could be transformed in ways we have yet to imagine. The questions we face today — such as whether rDNA can cure cancer, create universal medications, or enable species to thrive in space — are just the beginning!
-
-
#### References:
1. Purkait, Shuvam & Yousuf, Parvaiz. (2024). Futuristic Trends in Biotechnology RECOMBINANT DNA TECHNOLOGY AND ITS APPLICATIONS. 10.58532/V3BJBT5P6CH1.
diff --git a/wiki/blogposts/restrictionenz.md b/wiki/blogposts/restrictionenz.md
index d7fa7d2..b90a900 100644
--- a/wiki/blogposts/restrictionenz.md
+++ b/wiki/blogposts/restrictionenz.md
@@ -12,6 +12,8 @@ When a virus (specifically, a bacteriophage) attacks a bacterium, it inserts for
How does the restriction enzyme know where it should cut? Each restriction enzyme is designed such that it recognises and cuts only a unique DNA sequence. This unique sequence is known as a **recognition site**. These are characterised by 4-8 bases which are generally a palindrome (Example: GTAATG) or a mirror-palindrome (DNA sequences where a segment of nucleotides read the same forward and backwards on both strands, Example: GATATC-CTATAG (complementary base pairing)). For example, the EcoRI (from E.coli bacteria) enzyme recognises the GAATTC base pair sequence, the Alul (from A. luteus) enzyme recognises the AGCT base pair sequence, and the Haell (from H. aegyptius) enzyme recognises the GGCC base pair sequence.
+<img src = "https://static.igem.wiki/teams/5170/blogposts/restriction-enzyme-reference-microbe-notes.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
There is the possibility that similar base pair sequences exist in the bacterial DNA also. Bacteria use the **methylase enzyme** to add methyl groups to their DNA to prevent the restriction enzyme from cutting its own DNA.
How do we use Restriction Enzymes? It has various applications.
@@ -25,3 +27,4 @@ Presently, we know more than 3600 restriction enzymes from 250 different species
1. Roberts RJ, Restriction and modification enzymes and their recognition sequences, Science Direct, Jan 1980
2. Roberts RJ, Restriction endonucleases, CRC Critical Reviews in Biochemistry, 1976
3. Roberts RJ, How restriction enzymes became the workhorses of molecular biology, Proceedings of the National Academy of Sciences of the United States of America, 2005
+4. Image: Microbe Notes
diff --git a/wiki/blogposts/ribosomes_vidhi.md b/wiki/blogposts/ribosomes_vidhi.md
index a2a570b..7dd9088 100644
--- a/wiki/blogposts/ribosomes_vidhi.md
+++ b/wiki/blogposts/ribosomes_vidhi.md
@@ -20,14 +20,14 @@ In eukaryotic cells, ribosomes are synthesised in the [nucleolus](#), a dense st
In prokaryotic cells, ribosomes are free-floating in the cytoplasm. Prokaryotic cells do not have ER. They are composed of 65% rRNA and 35% proteins. They are 70S ribosomes, also consisting of 2 subunits – a larger subunit (50S) and a smaller subunit (30S).
+
+
The primary function of ribosomes is protein synthesis for the cell. Protein synthesis involves two steps – [transcription](#) and [translation](#) – following the [Central Dogma](#). Transcription occurs in the nucleus and involves the production of a [messenger RNA](#) (mRNA) molecule based on the [DNA](#) sequence in a given [gene](#) coding for a protein. This mRNA strand is picked up by the smaller subunit of the ribosome for the next step – translation.
Proteins are made of sequences of amino acids. The mRNA contains information about the sequence of amino acids required for making a specific protein. In the cell, amino acids are carried by [transfer RNA](#) (tRNA). tRNA acts as an adapter molecule – it reads the sequence of nucleotide bases on the mRNA and brings corresponding amino acids. Once the smaller subunit binds to mRNA, the larger subunit also arrives and catalyses the creation of [peptide bonds](#) between adjacent amino acids brought by tRNA. Ribosomes also play a part in protein folding – that is, the change of the protein into a 3-D structure that is biologically functional. This makes them a fascinating organelle to study.
Venkataraman Ramakrishnan, along with two others, won the Nobel Prize in Chemistry in 2009 for their research on the structure and function of the ribosome. In his words, ribosomes stand at the crossroads of biology – between the gene and what comes out of the gene.
-
-
#### References
1. Davidson, Michael W. (2015, November 13). *Ribosomes.* Molecular Expressions Cell Biology Florida State University.
2. [Ribosomes, Transcription and Translation, Nature Education](https://www.nature.com/scitable/topicpage/ribosomes-transcription-and-translation-14120660/)
diff --git a/wiki/blogposts/sdspage_soham.md b/wiki/blogposts/sdspage_soham.md
index 86b9f8b..a9ef7cd 100644
--- a/wiki/blogposts/sdspage_soham.md
+++ b/wiki/blogposts/sdspage_soham.md
@@ -18,20 +18,23 @@ SDS molecules have negatively charged ends which get attached to the positive ch
The SDS-treated protein samples are then placed on a **stacking gel** made of **acrylamide**. Gels are a meshwork of polymers with pores in them through which proteins can move. The stacking gel is layered on top of another acrylamide based gel called the **resolving gel** which has slightly different concentration (and hence pore size) and pH.
+<img src = "https://static.igem.wiki/teams/5170/blogposts/sds-page-williams-chemistry.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
The proteins, stacking gel and resolving gel are connected to electrodes and an electric field is applied. The stacking gel ensures that all samples reach the resolving gel at the same time, to account for differences in the time the sample was loaded.
Different proteins carrying different charges traverse dissimilar distances (towards the positive anode, since the samples have negative charge) when subjected to the field. Larger proteins travel less, as they face more resistance in moving through the pores of the resolving gel.
Proteins of different molecular weights appear as distinct **bands** on the gel, after staining with an appropriate dye such as [Coomassie Brilliant Blue (CBB)](#). Proteins with known molecular weights may also be added to the mixture (of proteins) to get a reference point for determining the mass of unknown proteins. This is called a **protein ladder** as it appears as a series of bands.
-SDS-PAGE is a fundamental process in **protein purification,** that is, separating a desired protein from an impure mixture. Proteins of interest can be located and separated using [Western Blotting](#) and [Immunocytochemistry](#).
+<img src = "https://static.igem.wiki/teams/5170/blogposts/sds-page-no-reference.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
-Proteins with known molecular weights may also be added to the mixture (of proteins) to get a reference point for determining the mass of unknown proteins. This is called a **protein ladder**
+SDS-PAGE is a fundamental process in **protein purification,** that is, separating a desired protein from an impure mixture. Proteins of interest can be located and separated using [Western Blotting](#) and [Immunocytochemistry](#).
#### Sources:
1. Sambrook J, Fritsch T, Maniatis T. 1989. Molecular Cloning: A Laboratory Manual. 1. New York: Cold Spring Harbor Laboratory Press.
2. Makoto Hagiwara, Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and western blotting analyses via colored stacking gels, Analytical Biochemistry, Volume 652, 2022, 114751, ISSN 0003-2697, https://doi.org/10.1016/j.ab.2022.114751.
+3. Image: Williams Chemistry
#### References:
diff --git a/wiki/blogposts/selectablemarker.md b/wiki/blogposts/selectablemarker.md
index 800a4be..384d7f5 100644
--- a/wiki/blogposts/selectablemarker.md
+++ b/wiki/blogposts/selectablemarker.md
@@ -10,6 +10,8 @@ Separating transformed cells on the basis of this newly acquired ability is call
Some of the most popular selectable markers are antibiotic resistance genes. Bacteria like *Escherichia coli* have always been favored for biotechnological uses. Hence, it is no surprise that antibiotic resistance is used to identify transformants from non-transformants. The NPT-II gene (neomycin phosphotransferase II) confers resistance to bacteria against the antibiotics kanamycin and neomycin.
+
+
How exactly does this process of selection of transformants work? Consider the famous **pBR322 plasmid,** designed by Bolivar and Rodriguez (hence the name pBR322). It contains ampicillin and tetracycline resistance genes. If the gene of interest is inserted in the region of, say, tetracycline resistance, the recombinants will only be resistant to ampicillin - because the tetracycline resistance gene gets interrupted. This is called **insertional inactivation**.
In the antibiotic-based screening approach, the recombinants are grown on an ampicillin-containing master plate. A replica of the colony is created using a nitrocellulose membrane. This is transferred to a medium containing both ampicillin and tetracycline. This process is called replica plating. Only the non-recombinants grow (as the recombinants have lost tetracycline resistance, and the non-transformants do not have ampicillin resistance as they lack pBR322).
diff --git a/wiki/blogposts/tauopathies.md b/wiki/blogposts/tauopathies.md
index cdd4107..d8695a2 100644
--- a/wiki/blogposts/tauopathies.md
+++ b/wiki/blogposts/tauopathies.md
@@ -10,6 +10,8 @@ Tau are microtubule associated proteins that are responsible for stabilisation o
**Neurofibrillary tangles (NFTs)** are known largely as a biomarker for Alzheimer’s Disease, however they develop in other tauopathies as well. In Alzheimer’s, the tau protein gets hyperphosphorylated (and is called p-Tau), and subsequently forms neurofibrillary tangles and paired helical filaments. These hamper axonal functions and lead to the degeneration of neurons. Interestingly, factors released by the presence of [beta-amyloid aggregates](#) (another biomarker of Alzheimer’s) may trigger p-Tau hyperphosphorylation and misfolding. The presence of beta-amyloid greatly impacts the neuron to neuron transport of the misfolded p-Tau protein. Hence, NFTs and p-Tau proteins are considered key biomarkers for Alzheimer’s, the most common among the tauopathies.
+<img src = "https://static.igem.wiki/teams/5170/blogposts/export202407280116098149.png", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
Treatment of tauopathies focuses on decreasing protein aggregation and neurofibrillary tangles. The use of [aptamers](#) to bind to sites on the p-Tau protein in order to prevent phosphorylation is also being studied.
#### References:
diff --git a/wiki/blogposts/transcription.md b/wiki/blogposts/transcription.md
index 5b5200f..546917c 100644
--- a/wiki/blogposts/transcription.md
+++ b/wiki/blogposts/transcription.md
@@ -10,12 +10,12 @@ DNA is normally present in a double helix, but for the purpose of transcription,
A **primer molecule** attaches complementary nucleotides to the template strand to begin the transcription. RNA Polymerase continues to attach complementary bases and the transcribed mRNA begins to form. The bases are added on the 3’ end of the transcript, that is, polymerisation proceeds in the 5'-3' direction. The 5’ end is formed by the primer nucleotides. The process continues until the RNA Polymerase encounters a segment of DNA called the **terminator** sequence. This triggers the release of the RNA Polymerase from the transcription initiation complex and the process of transcription ends.
+
+
Other than its role in gene expression, transcription also plays an important role in **gene regulation**. Regulation is the control of quantity, location and appropriate timing for the production of genes. Transcription factors play an important role here since they are responsible for choosing which sequences should be transcribed. The transcription process does not begin without the binding of a transcription factor, hence they control the timing of the process. There are other factors which play a role in gene expression regulation, such as the **operon system** in prokaryotes.
Transcription is just the initial step of gene expression and where the major part of gene regulation takes place. It is followed by [translation](#).
-
-
#### References
1. Crick F, On Protein Synthesis, Symposia for the Society of Experimental Biology, (1958)
2. Latchman D, Transcription Factors: an Overview, Int J Exp Pathol. (1993)
diff --git a/wiki/blogposts/transformation_chandana.md b/wiki/blogposts/transformation_chandana.md
index d43df26..f01ff42 100644
--- a/wiki/blogposts/transformation_chandana.md
+++ b/wiki/blogposts/transformation_chandana.md
@@ -8,6 +8,8 @@ date: 7 September 2024
Bacterial Transformation is a process by which a bacterium takes up foreign [DNA](#) from its surroundings through the cell membrane, and integrates it into its own DNA. The foreign DNA material may be present as partially degraded fragments of dead cells or can be artificially introduced to it. For this process to occur, the bacterium cell must be in a state called "[competent state](#)" (that is, the cell membrane must be permeable), which, again, can occur naturally, or be artificially induced by physical chemical methods or electrical methods. The most common way of creating competent cells is by treating them with salts of divalent cations (such as calcium and magnesium chloride) followed by rapid heating and cooling (called **heat shock**).
+<img src = "https://static.igem.wiki/teams/5170/blog-images/transduction.png", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
Transformation was first discovered by Frederick Griffith in 1928, who observed that non-damaging bacteria could be ‘transformed’ into damage-inducing ones by exposing them to heat-killed strains of the latter.
It is believed that transformation occurs naturally to repair DNA damages, and it simultaneously generates **genetic diversity**. This phenomenon is exciting because it gives us a starting idea on how to achieve [DNA cloning](#) – since our desired [gene](#) can be replicated if introduced in a bacterium. In some cases, bacterial transformation can also be used to identify certain genes – because the introduced DNA can cause a [mutation](#) in the said gene, altering the characteristics of the bacterium which can be observed.
diff --git a/wiki/blogposts/translation_chandana.md b/wiki/blogposts/translation_chandana.md
index 73dc659..04f1400 100644
--- a/wiki/blogposts/translation_chandana.md
+++ b/wiki/blogposts/translation_chandana.md
@@ -23,9 +23,9 @@ To understand translation, we need to know few important terms -
The codon gives instructions regarding which amino acids to be added. The ribosomes bind to the incoming mRNA. The anticodon in the tRNA binds to corresponding codon in the mRNA, and the attached amino acids form [peptide bonds](#), catalysed by the rRNA present in the ribosome. This facilitates the formation of a polypeptide which later folds to form a protein. Translation initiates at the start codon (AUG) and terminates at the stop codons (UAA, UAG, UGA).
-The process of adding amino acids continues till the complete mRNA is translated (that is, a stop codon is reached). Subsequently, the mRNA and the sequence of amino acids (polypeptide) is released from the ribosome. The polypeptide undergoes folding and/or modification in the cytosol or endoplasmic reticulum, forming a functional protein. After this, the protein can stay in the cytosol (liquid portion of cytoplasm) or can go to any of the cell organelles like mitochondria, chloroplasts, etc.
+
- 
+The process of adding amino acids continues till the complete mRNA is translated (that is, a stop codon is reached). Subsequently, the mRNA and the sequence of amino acids (polypeptide) is released from the ribosome. The polypeptide undergoes folding and/or modification in the cytosol or endoplasmic reticulum, forming a functional protein. After this, the protein can stay in the cytosol (liquid portion of cytoplasm) or can go to any of the cell organelles like mitochondria, chloroplasts, etc.
#### References:
diff --git a/wiki/blogposts/ups.md b/wiki/blogposts/ups.md
index b8ceeb0..294f465 100644
--- a/wiki/blogposts/ups.md
+++ b/wiki/blogposts/ups.md
@@ -11,10 +11,14 @@ Luckily , our body has developed checks for this sort of misfolding . One of the
There are large, barrel shaped molecules in our body known as **proteosomes** whose function is to break down proteins. But the question arises, if all our internal processes are facilitated by proteins, how do the proteosomes know which ones to break down and which ones to ignore? They do so with the help of a chemical tag that they recognise. The name of this molecule is **ubiquitin**, which is another protein (a rather ubiquitous one - hence the name) that is virtually indistinguishable across all life forms.
The actual process, however is a tad more complicated, involving three enzymes. First, ubiquitin is activated by being attached to the ubiquitin-activating enzyme, E1. The ubiquitin is then transferred to a second enzyme, called ubiquitin-conjugating enzyme (E2). The final transfer of ubiquitin to the target protein is then mediated by a third enzyme, called **ubiquitin ligase or E3**. It is after this that the protein is recognised by the proteasome and hence degraded. This is known as the Ubiquitin-Proteasome System (UPS), and the **Nobel Prize in Chemistry in 2004** was awarded jointly to Aaron Ciechanover, Avram Hershko and Irwin Rose for the discovery of ubiquitin-mediated protein degradation.
+
+<img src = "https://static.igem.wiki/teams/5170/blogposts/ups-and-why-it-won-nobel-ref-pinterest.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
But why was this discovery that important? To answer this, its important to look at the history of protein degradation research. A number of simple protein-degrading enzymes were already known. One example is trypsin, which in the small intestine breaks down proteins in our food to amino acids. Likewise, a type of cell organelle, the lysosome, in which proteins absorbed from outside are broken down, had long been studied. Common to these processes is that they do not require energy in order to function.
Experiments as long ago as the 1950s showed, however, that the breakdown of the cell’s own proteins does require energy. This long puzzled researchers, and it is precisely this paradox, or rather its explanation that won the 2004 Nobel Prize in Chemistry: that the breakdown of proteins within the cell requires energy while other protein degradation takes place without added energy as illustrated earlier.
+
+<img src = "https://static.igem.wiki/teams/5170/blogposts/ups-system-ref-lifesensors.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
This discovery hence paved the way for a novel drug delivery system that goes by the name of **PROTAC (Proteolysis Targeting Chimera)**. This is a synthetic molecule that not only quickens the transfer of ubquitin to the target protein but also makes it more efficient. But how does it do it?
@@ -28,4 +32,5 @@ In short, PROTACs and the ubiquitin-proteasome system (UPS) make a powerful comb
1. Park, J., Cho, J., & Song, E. J. (2020). Ubiquitin-proteasome system (UPS) as a target for anticancer treatment. Archives of pharmacal research, 43(11), 1144–1161.
2. OlguÃn H. C. (2022). The Gentle Side of the UPS: Ubiquitin-Proteasome System and the Regulation of the Myogenic Program. Frontiers in cell and developmental biology, 9, 821839.
3. Kresge, Nicole & Simoni, Robert & Hill, Robert. (2006). The Discovery of Ubiquitin-mediated Proteolysis by Aaron Ciechanover, Avram Hershko, and Irwin Rose. The Journal of biological chemistry. 281. e32.
+4. Images: LifeSensors and Pinterest
diff --git a/wiki/blogposts/westernblot.md b/wiki/blogposts/westernblot.md
index f97991b..0d0656b 100644
--- a/wiki/blogposts/westernblot.md
+++ b/wiki/blogposts/westernblot.md
@@ -10,11 +10,14 @@ Why is Western Blotting important? It helps in the detection specific proteins i
Interestingly, the name Western Blotting comes from a similar technique used for the transfer of DNA strands - called Southern Blotting after the scientist Robert Southern. The analogous techniques for RNA and proteins were simply named Northern and Western - and not because they were after scientists by those names!
-The membrane (on to which proteins are transferred) is between the gel surface and positive electrode in a sandwich. After SDS-PAGE, all the proteins have already acquired a uniform negative charge. A fiber pad or sponge is kept at positive end (the top) and filter papers are used to protect the gel and blotting membrane.
-Two things are important here - close contact of the gel and the membrane (to get a clear image), and the correct placement and orientation of the membrane between the gel and the positive electrode.
+The membrane (on to which proteins are transferred) is between the gel surface and positive electrode in a sandwich. After SDS-PAGE, all the proteins have already acquired a uniform negative charge. A fiber pad or sponge is kept at positive end (the top) and filter papers are used to protect the gel and blotting membrane. Two things are important here - close contact of the gel and the membrane (to get a clear image), and the correct placement and orientation of the membrane between the gel and the positive electrode.
+
+<img src = "https://static.igem.wiki/teams/5170/blogposts/western-blotting.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
Western Blotting is followed up with **[immunostaining](#)** to identify where the protein of interest is. In simple words, it makes use of the specificity and fidelity of antigen-antibody interactions. An antibody specific to the protein of interest is made to bind with it, and a secondary antibody binds to the primary antibody and either gives of a fluorescent or radioactive signal (**autoradiography**) or is conjugated with an enzyme which can be quantified using an assay. For instance, the enzyme horseradish peroxidase acts on substrate TMB in the presence of hydrogen peroxide to give a bright blue oxidised product.
+<img src = "https://static.igem.wiki/teams/5170/blogposts/western-blotting-ref-mybiosource.webp", style = "max-height: 300px; max-widht: auto; display: block; margin-left: auto; margin-right: auto;}" alt = "gene">
+
The membrane used in Western Blotting is broadly of two types:
1. **PVDF (Polyvinylidene Difluoride):** has better mechanical support, allows reprobing and storage, but background noise is higher which necessitates good washing
@@ -26,4 +29,5 @@ The membrane used in Western Blotting is broadly of two types:
#### References:
1. Mahmood, T., & Yang, P. C. (2012). Western blot: technique, theory, and trouble shooting. North American journal of medical sciences, 4(9), 429–434.
+2. Image: MyBioSource
diff --git a/wiki/pages/home.html b/wiki/pages/home.html
index f3b064e..cb3d89f 100644
--- a/wiki/pages/home.html
+++ b/wiki/pages/home.html
@@ -78,10 +78,8 @@
<!-- Carousel Inner -->
<div class="carousel-inner h-100">
- <div class="carousel-item active" style="background-image: url('https://static.igem.wiki/teams/5170/slide3.webp');">
+ <div class="carousel-item active" style="background-image: url('https://static.igem.wiki/teams/5170/videos/whatsapp-video-2024-10-02-at-4-46-59-pm.gif');">
<div class="carousel-caption">
- <h1>AptalXero</h1>
- <h3>iGEM IISc Bengaluru</h3>
<!-- Uncomment the following lines if you want to include buttons -->
<!-- <button type="button" class="btn btn-outline-light btn-lg">Button 1</button>
<button type="button" class="btn btn-primary btn-lg">Button 0</button> -->
diff --git a/wiki/pages/team.html b/wiki/pages/team.html
index e03d1bf..d79aac4 100644
--- a/wiki/pages/team.html
+++ b/wiki/pages/team.html
@@ -52,7 +52,7 @@
<div class="card">
<img class="card-img-top" src="https://static.igem.wiki/teams/5170/team/subhanan.webp" alt="" style="height: 400px; width: 100%; object-fit: cover; overflow:hidden;">
<div class="card-body">
- <h4 class="card-title text-center">Subhanan Banarjee</h4>
+ <h4 class="card-title text-center">Subhanan Banerjee</h4>
<p class="card-text text-center">Team Leader</p>
</div>
</div>
--
GitLab