diff --git a/wiki/blogposts/aminoacids.md b/wiki/blogposts/aminoacids.md
new file mode 100644
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+---
+title: Amino Acids and Peptide Bonds
+author: Mihir Kapse
+date: 2 October 2024
+---
+
+The word ‘proteins’ pops up everywhere in many different conversations. Sometimes it is about food diet and a few times it might be about biomolecules, diseases, or genetic material. These all have proteins as a major component. Proteins are nothing but bio-polymers of a type of **amino acid** called alpha-amino acids.
+
+Fundamentally, amino acids are organic compounds that have both functional groups: **amino and carboxyl.** Depending on the relative position of these two functional groups, amino acids are classified into various types. All biological systems mainly consist of alpha-amino acids. They are of extreme importance to all biological life.
+
+In 1806, French chemists Vauquelin and Robiquet successfully isolated Asparagine, the first amino acid to be discovered. Later on in 1810, another amino acid Cystine was discovered. Subsequently, more and more amino acids were discovered. Currently, we know that over 500 amino acids exist in nature.
+
+For us, there are majorly two types of amino acids: essential and non-essential amino acids. Essential are the ones that our body cannot synthesise on its own and so we rely on diet. On the other hand, non-essential amino acids are the ones that our body can synthesize. Amino acids are found everywhere in our body. Enzymes, hormones, protein synthesis, neurotransmitters, etc all require amino acids.
+
+Beyond their role as residues in protein, amino acids participate in other biological processes such as neurotransmitter transport and biosynthesis. Amino acids are also added to animal feed to fulfil animal’s requirements for their essential amino acids. Because of their chelating ability, they are sometimes used in fertilizers to facilitate the delivery of minerals to plants.
+
+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.
+
+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:
+1. Muller, P.. Glossary of terms used in physical organic chemistry. Pure and Applied Chemistry. 1994
+2. Nelson DL, Cox MM. Principles of Biochemistry (4th ed.). New York: W. H. Freeman. 2005
+3. Flissi, Areski; Ricart, Emma; Campart, Clémentine; Chevalier, Mickael; Dufresne, Yoann; Michalik, Juraj; Jacques, Philippe; Flahaut, Christophe; Lisacek, Frédérique; Leclère, Valérie; Pupin, Maude. Norine: update of the nonribosomal peptide resource. Nucleic Acids Research. 2020
+4. Vauquelin LN, Robiquet PJ. The discovery of a new plant principle in Asparagus sativus. Annales de Chimie. 1806
+5. Wollaston WH. On cystic oxide, a new species of urinary calculus. Philosophical Transactions of the Royal Society. 1810
+6. Leuchtenberger W, Huthmacher K, Drauz K. "Biotechnological production of amino acids and derivatives: current status and prospects". Applied Microbiology and Biotechnology. November 2005
+7. Ashmead HD. Foliar Feeding of Plants with Amino Acid Chelates. Park Ridge: Noyes Publications. 1986
+
diff --git a/wiki/blogposts/gene.md b/wiki/blogposts/gene.md
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+++ b/wiki/blogposts/gene.md
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+---
+title: Gene
+author: Mihir Kapse
+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.
+
+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:
+1. **Coding genes:** Genes that contain the instructions to make a protein are called coding genes. These regions are [transcribed](#) into [messenger RNA](#) by the RNA polymerase, which then gets transported to [ribosomes](#) where protein synthesis takes place. This process is called gene expression.
+2. **Non-coding genes:** Genes that do not code for proteins are called non-coding genes. Instead, they produce functional RNA molecules, like [ribosomal RNA](#) and [transfer RNA](#). Some RNAs produced from these genes regulate gene expression, some are essential for RNA splicing, and some play a crucial role in genome stability.
+
+During the process of reproduction, genes carry the traits and other necessary information from the parent to the offspring. These genes make up different DNA sequences, together called a genotype. The genotype of an individual is very specific with respect to the gene pool of the population of a given species. It carries information for everything, hair colour, eye colour, height, skin colour, and whatnot. Genes are the ultimate source of information for the zygote so formed for its growth and development.
+
+Sometimes, during [DNA replication](#), a gene can acquire mutations in its sequence. Subsequently, these cause changes in individuals which can further lead to the evolution of species. Humans share about 98-99% genes with chimpanzees. This merits the fact that humans and chimpanzees have evolved from a common ancestor.
+
+As an interesting fact, for many years, companies were able to patent human genes. Around 20% of the human genome was under patent by 2005. Fortunately, in 2013, the U.S. Supreme Court stopped it.
+
+#### References:
+1. Orgogozo V, Peluffo AE, Morizot B. The "Mendelian Gene" and the "Molecular Gene": Two Relevant Concepts of Genetic Units. Current Topics in Developmental Biology. 2016
+2. Noble D. "Genes and causation". Philosophical Transactions. Series A, Mathematical, Physical, and Engineering Sciences. 2008
+3. Johannsen W. Elemente der exakten Erblichkeitslehre [Elements of the exact theory of heredity] (in German). Jena, Germany: Gustav Fischer. 1909
+4. Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P. Molecular Biology of the Cell (Fourth ed.). New York: Garland Science. 2002
diff --git a/wiki/pages/engineering.html b/wiki/pages/engineering.html
index 4c76e6d0772777c378d2687d4a5d6daafda14782..bf90b0da3ecf6bd09f7196930641d46bb265f2dd 100644
--- a/wiki/pages/engineering.html
+++ b/wiki/pages/engineering.html
@@ -5,16 +5,92 @@
{% block page_content %}
-<div class="row mt-4">
- <div class="col">
- <div class="bd-callout bd-callout-info">
- <h4>Silver Medal Criterion #1</h4>
- <p>Demonstrate engineering success in a part of your project by going through at least one iteration of the engineering design cycle. This achievement should be distinct from your Contribution for Bronze.</p>
- <p>If you plan to show engineering success by creating a new Part that has been shown to work as expected, you must document your contribution on the Part's Main Page on the <a href="https://parts.igem.org/Main_Page">Registry</a> for your team to be eligible for this criteria.</p>
- <hr>
- <p>Please see the <a href="https://competition.igem.org/judging/medals">2024 Medals Page</a> for more information.</p>
- </div>
- </div>
-</div>
+
+<style>
+ body {
+ background-color: #D2B48C; /* To match the background color in your image */
+ }
+ table {
+ width: 60%;
+ border-collapse: collapse;
+ margin: 20px auto; /* Center the table horizontally */
+ font-family: Arial, sans-serif;
+ }
+ th, td {
+ padding: 10px;
+ border: 1px solid black; /* Add lines between cells */
+ text-align: center; /* Center-align the content */
+ }
+ th {
+ background-color: #4CAF50;
+ color: white;
+ }
+
+ p{
+ text-align: justify;
+ padding: 1rem;
+ }
+
+ h1, h2, h3, h4, h5, h6 {
+ text-align: center;
+ padding: 1rem;
+ }
+</style>
+
+</head>
+<body>
+ <div class="container"><div class="row justify-content-center">
+ <div class="col-lg-10">
+ <h1>Engineering Cycles</h1>
+ <div style="height: 3rem;"></div>
+ <h2>Experiment: Predicting the structure of pTau with several combinations of phosphorylation sites</h2>
+ <p><strong>DESIGN</strong>: We can model a phosphorylation site (mostly Threonine or Serine, although Tyrosine also potentially phosphorylates) with a phosphomimetic amino acid (primarily Aspartic acid or Glutamic acid) which mimics the charge distribution or structure parameters. Thus, some Alzheimer’s marker phosphorylation can be incorporated into the protein by phosphomimetics to mimic the same conditions.</p>
+ <p><strong>BUILD</strong>: We selected a few sites of relevance: 231T, 198S, 199S, 205S etc and replaced with Aspartic acid.</p>
+ <p><strong>TEST</strong>: We obtained the structures using ChimeraX and AlphaFold by using energy minimisation option.</p>
+ <p><strong>LEARN</strong>: The structures are completely different from the initial intrinsically disordered. The arising hydrophobicity can be correlated to the tendency of aggregation.</p>
+ <div style="height: 3rem;"></div>
+ <h2>Experiment: Preparation of competent BL21 DE3 E. coli cells</h2>
+ <p><strong>DESIGN</strong>: Proliferation of BL21 E. coli cells, and modifying the newly formed cells to make competent cells. Competent cells can take up plasmids and can express them.</p>
+ <p><strong>BUILD</strong>: We used chemical method of producing competent cells. The preformed BL21 cells (brought from another lab) were propagated and then subjected to buffers containing RbCl, CaCl2, PIPES, etc. to make them competent to induce plasmid and express it.</p>
+ <p><strong>TEST</strong>: Transformed plasmid, specific for expression in BL21 cells, and plated it on non-antibiotic LB agar plate. Control was setup, which involved transformation of original BL21 (from which it was propagated) with the same plasmid.</p>
+ <p><strong>LEARN</strong>: We found that the original stock of BL21 had proper growth, which approved the functionality of the plasmid. But, unfortunately there was no growth in the prepared competent cell. This might have happened due to improper methodologies or slight difference in buffer. Utmost care needs to be taken during competent cell preparation. There is also a high chance of contamination, and it involves destruction of cells.</p>
+ <div style="height: 3rem;"></div>
+ <h2>Experiment: Transformation of Tau 441 plasmid into BL 21 DE3 E. coli.</h2>
+ <p><strong>DESIGN</strong>: Transformation of Tau/pET29b (Addgene #16316) plasmid into BL 21 E. coli using heat shock method.</p>
+ <p><strong>BUILD</strong>: We modified some aspects of a general heat-shock method of plasmid transformation. The protocol we followed can be found in the protocols section.</p>
+ <p><strong>TEST</strong>: We grew the primary culture of bacteria in Kanamycin antibody. The plasmid, which has KanR gene, expresses in Kanamycin antibody.</p>
+ <p><strong>LEARN</strong>: We saw proper growth of Bacterial culture, which meant that the bacteria successfully took up the plasmid and could express it. Afterwards we also extracted protein from it, which again proves its success.</p>
+ <div style="height: 3rem;"></div>
+ <h2>Experiment: Expression and purification of Human Tau 441 protein.</h2>
+ <p><strong>DESIGN</strong>: After successful transformation, the bacterial culture can express the protein. The protein can be extracted and purified to obtain pure protein, free from contamination. This protein can be used further in testing and phosphorylation.</p>
+ <p><strong>BUILD</strong>: The protein could be expressed using IPTG, in E. coli bacterial culture. We modified some aspects of a general protein purification. The protocol we followed can be found in the protocols section. We could use Ni-NTA gravity column method of purification, due to availability of His tag in our construct.</p>
+ <p><strong>TEST</strong>: We ran SDS gel to obtain protein bands. We compared it to the standard protein marker. The protein, conjugated with His tag, needs to come at around 50kDa range.</p>
+ <p><strong>LEARN</strong>: We could obtain a single protein band in the eluted fraction. We did find bands in the same range in Wash fraction and slightly in flow through, which concludes that this might not be the efficient method of purification, in terms of wastage. But we are sure that this is a fairly good method, in terms of the quality of protein obtained.</p>
+ <div style="height: 3rem;"></div>
+ <h2>Experiment: To show the presence of 231pTau and binding of aptamers to it, simultaneously.</h2>
+ <p><strong>DESIGN</strong>: Since the aptamers bind with the protein pTau, we expect a shift or smear of the protein bands when the protein incubated with the aptamer at optimal concentration is loaded on a native gel made with TBE. Thus, if we do a WB with the aptamer incubated protein, there will be an observable compared with the case of no aptamers.</p>
+ <p><strong>BUILD</strong>: We improvised the standard protocol of EMSA, instead of using autoradiography we used visualisation of the protein using the antibody conjugate (pTau rabbit monoclonal and anti-rabbit hrp-conjugated).</p>
+ <p><strong>TEST</strong>: We did Western blot with the protein incubated with the aptamers at 0.1 micromolar concentration.</p>
+ <p><strong>LEARN</strong>: We found that although the smear is evident, there is a significant background. This is because of using skimmed milk as blocking agent, which contains casein. Casein is a phosphoprotein and the pTau antibody may have some non-specific binding tendency to Casein as an Ab selected for a phosphoprotein may have non-specific binding with phosphoproteins as the phosphorylated moiety is always either of Threonine, Serine or Tyrosine.</p>
+ <div style="height: 3rem;"></div>
+ <h2>Experiment: Using random mutagenesis in SELEX for quicker results.</h2>
+ <p><strong>DESIGN</strong>: SELEX relies on randomness, as the chances of an optimal sequence to bind with the target increases with large combinations. Thus, if the randomisation is done at a greater degree, in each round of SELEX on a partition of the eluded aptamers, the selection of Aptamers may be accomplished in exponentially lesser time. We found that the incorporation of non-conventional bases like dPTP and oxo-GTP can cause random point mutations at an incredible level of 10% after a few cycles of PCR followed by asymmetric PCR. We needed a high mutation rate due to small size of the aptamers.</p>
+ <p><strong>BUILD</strong>: Since our Aptamers were already selected for the target by 17 cycles by the original authors, we planned to perform the same with a different sample DNA. However, on analysing the aptamers, we hypothesised that high G repeats may have been responsible for a better binding to the target. dPTP causes G biased transitions.</p>
+ <p><strong>TEST</strong>: On performing the PCR, we couldn’t observe the bands of the PCR product in the gel.</p>
+ <p><strong>LEARN</strong>: The reasons could be firstly, incorporation of non-conventional bases might slow down the action of normal Taq-polymerase. Secondly, the dPTP or oxo-GTP incorporated DNA may not be a perfect helix, as these bases exist in tautomeric form.</p>
+ <div style="height: 3rem;"></div>
+ <h2>Experiment: Click reaction of C8-Alkyne dCTP with [S, R, S]-AHPC-PEG1-Azide (VHL Ligand)</h2>
+ <p><strong>DESIGN</strong>: C8-Alkyne dCTP may undergo cycloaddition with VHL ligand, having an azide label. This product after HPLC purification can be incorporated into an aptamer by terminal transferase. The ligand can help localising the Aptamer around VHL E3 ubiquitin ligase, leading to polyubiquitination of the target.</p>
+ <p><strong>BUILD</strong>: We set the protocols for accomplishing click reaction of C8-Alkyne dCTP with [S, R, S]-AHPC-PEG1-Azide (VHL Ligand). We also modelled the structure of the product.</p>
+ <p><strong>TEST</strong>: We did the calculation of the radius of gyration and other aspects of the molecule by computer simulation.</p>
+ <p><strong>LEARN</strong>: We got the radius of gyration to be 16.54652 Angstroms, which shows that the final molecule is highly coiled and thus, may have unexpected behavior.</p>
+ <div style="height: 3rem;"></div>
+ <h2>Experiment: Testing of software of previous iGEM team and troubleshooting of several bugs and errors.</h2>
+ <p><strong>DESIGN</strong>: Run MAWS on the VQIINK part of 2mz7 pdb (residues 275-280) and get an Aptamer Sequence.</p>
+ <p><strong>BUILD</strong>: Perform the necessary improvements to the software as mentioned in the AptaLoop documentation. Create a GUI (tkinter based or web based, preferably web-based) of the software for the help of others who will use this tool. Understanding what sqm actually does, and what is exactly stored in it, along with the error messages shown by it.</p>
+ <p><strong>TEST</strong>: Run the examples, to get an idea what is happening in each module. Chopped down 2MZ7 PDB to get the said hexapeptide (VQIINK). Added H atoms wherever was missing using PyMol to get a working.</p>
+ <p><strong>LEARN</strong>: Residues more than 10 did not work. Infinite pause time error was occurring because of an os.waitpid() function. Duplicate atom warning was coming up. Understood which Aptamer sequence to work with given a whole pool is generated in output. Need to start building the part and integrate other tools, and also the GUI.</p>
+ </div></div></div><div style="height: 10rem;"></div>
+
{% endblock %}
diff --git a/wiki/pages/team.html b/wiki/pages/team.html
index 19bc257365e7c418458ae389176fad8259139b99..e03d1bf077454c5b27e2189631711da9cb93e74c 100644
--- a/wiki/pages/team.html
+++ b/wiki/pages/team.html
@@ -354,6 +354,7 @@
<li>Mukta Khanolkar</li>
<li>Jashandeep Thind</li>
<li>Abhay Mahata</li>
+ <li>Krishna Bhikadiya</li>
</ul>
</div>
<div class="col-md-3">