diff --git a/wiki/pages/experiments.html b/wiki/pages/experiments.html
index 0d938bb27a81a94c5c7ea7b8fd651da09bc33525..58ff0b6b05ad3f0ae0b3fed8cbb0a0f9332f5f6c 100644
--- a/wiki/pages/experiments.html
+++ b/wiki/pages/experiments.html
@@ -57,7 +57,7 @@
                         </ul>
 
                     </aside>
-
+                
                 </div>
                 <div class="col-lg-7">
                     <!--Experiment Aims-->
@@ -78,30 +78,13 @@
                     <div id="second">
                         <h2 class="font-weight-extra-normal text-7 mb-2 bigger-text">
 
-                            <strong class="font-weight-extra-bold">Choosing Target genes</strong>
+                            <strong class="font-weight-extra-bold">Choosing Target Genes</strong>
                         </h2>
                         <h4 class="font-weight-bold custom-heading">
                             <i>PETase</i>
                         </h4>
                         <p class="bigger-text">
-                            PETase is an enzyme that belongs to the esterase class of enzymes. It catalyzes the breakdown of
-                            polyethylene terephthalate (PET) plastic through hydrolysis, resulting in the formation of monomeric
-                            mono-2-hydroxyethyl terephthalate (MHET), BHET (bis(2-hydroxyethyl) terephthalate), and
-                            terephthalic acid (TPA), opening up possibilities for biological PET recycling and degradation. The
-                            most popular PETase enzyme was identified in 2016 from a strain of bacteria called Ideonella
-                            sakaiensis 201-F6, found in sludge samples collected near a PET bottle recycling site in Japan
-                            (Yoshida). IsPETase studied by Japanese groups for several years showed that it has more tolerance
-                            for catalytic activities to degrade PET plastic in variable environments (citations from intro).
-                            IsPETase has been confirmed to have the highest PET degradation activity under mild conditions of all
-                            PET-degrading enzymes from different microorganisms, as evidenced by its structure and chemical
-                            bonding (Anuar). One of the key factors to this is the enzyme's structure, in which IsPETase has a
-                            broader and more open active-site cleft compared to other enzymes like cutinases, which allows it to
-                            accommodate PET molecules more effectively. The 3 amino acid mutations our team created will widen
-                            the cleft, allowing the catalytic activities to perform easier and faster, enhancing the overall
-                            efficiency of PET product recycling (GAO). The wider substrate-binding pocket of PETase is critical
-                            for PET hydrolysis, which is the major process of breaking down plastics into monomeric blocks.
-                            Furthermore, IsPETase possesses two disulfide bonds in its active site, contributing to its efficiency
-                            in PET substrate binding.
+                            PETase is an enzyme that belongs to the esterase class of enzymes. It catalyzes the breakdown of polyethylene terephthalate (PET) plastic through hydrolysis, resulting in the formation of monomeric mono-2-hydroxyethyl terephthalate (MHET), BHET (bis(2-hydroxyethyl) terephthalate), and terephthalic acid (TPA), opening up possibilities for biological PET recycling and degradation. The most popular PETase enzyme was identified in 2016 from a strain of bacteria called <i>Ideonella sakaiensis 201-F6</i> , found in sludge samples collected near a PET bottle recycling site in Japan (Yoshida,2021). <i>is</i>
                         </p>
                         <p class="bigger-text">
                             After many studies and experiments, several characteristics make IsPETase a promising candidate for
@@ -143,21 +126,24 @@
                                    <i>Making T7-IsPETase plasmid</i>
                                </h4>
                                    <img src="https://static.igem.wiki/teams/5094/experiment/making-t7-ispetase-plasmid.jpg" alt="making-t7-ispetase-plasmid" width="800">
-
+                                    <p class = "bigger-text">
+                                        Fig. 1: Making T7-IsPETase plasmid diagram
+                                    </p>
 
                                <h4 class="font-weight-normal custom-heading">
                                    <i>PCR via PET synthesized from a biotech company </i>
-                              
+                             
                                </h4>
                                    <p class="bigger-text">
                                        We synthesized the IsPET gene via PCR protocol. We designed the forward primer flanked with the BamHI enzyme recognition site and the reverse primer flanked with the HindIII enzyme recognition site. Our team purchased the synthesized IsPETase gene from the Mission Biotech Company used as the DNA template, and a PCR experiment was performed to amplify the IsPETase gene flanked with BamHI and HindIII enzyme cut sites at both ends of the gene.
                                    </p>
+                            <!--
                                    <h5 class="font-weight-lighter">
                                        <i>Proof of concept: PCR products</i>
                                    </h5>
                                     <img src="https://static.igem.wiki/teams/5094/experiment/fig1.png" alt="fig1" width="800">
-
-
+                                   
+                                -->
                               
                                <h4 class="font-weight-normal custom-heading">
                                    <i>Double enzyme digestions on PCR products                                    </i>
@@ -181,14 +167,14 @@
                                     Transform the ligated T7-IsPETase plasmid into DH5ɑ bacterial competent cells, which can do the LB-amp plate selection. The bacterial colonies grow on the LB-amp plates indicating that they contain our team’s cloned plasmids. This can be done by heat-shocking the bacterial competent cells with the cloned plasmids and then allowing them to recover and grow on LB-amp selected plates. 
                                    </p>
 
-
+                                   <!--
                                <h4 class="font-weight-normal custom-heading">
                                    <i>Inoculate single bacterial colony</i>
                                </h4>
                                    <p class="bigger-text">
                                     Inoculate several bacterial colonies on LB-amp plates and broth, which suggests those bacterial colonies contain our team’s T7-IsPETase plasmid with an amp-resistant gene. This allows the bacteria to grow and multiply, amplifying the cloned DNA in our team’s T7-IsPETase plasmid. Then, plate the transformed bacteria on LB-AMP plates and broth. The ampicillin in the plates selects bacteria that have taken up the plasmid, as the plasmid contains an ampicillin resistance gene. Our team makes those single bacterial colonies into 25% glycerol stocks and keeps them at -80 degrees. 
                                    </p>
-
+                                -->
 
                                <h4 class="font-weight-normal custom-heading">
                                    <i>Bacterial Plasmid Extraction</i>
@@ -204,9 +190,11 @@
                                    <p class="bigger-text">
                                     We do PCR again to confirm bacterial colonies containing our team’s T7-IsPETase plasmid: After selecting colonies on the LB-AMP plates, perform PCR using primers specific to the cloned IsPETase gene to confirm the presence of the desired insert in the plasmid. This helped verify the success of the cloning process (amplification of the targeted DNA segment).
                                    </p>
-                                   <h5 class="font-weight-lighter">
-                                       <i>Proof of concept:</i>
-                                   </h5>
+                                <h4 class = "font-weight-normal custom-heading">
+                                    <i>Proof of Concept:</i>
+                                </h4>
+                             
+                                   <img src="https://static.igem.wiki/teams/5094/experiment/fig1.png" alt="fig1" width="800">
                                    <img src="https://static.igem.wiki/teams/5094/experiment/fig2.png" alt="fig2" width="800">
 
 
@@ -215,193 +203,204 @@
                        <!--Making the pGal 1,10-IsPETase Plasmid-->
 
 
-                           <h4 class="font-weight-bold custom-heading">
-                                   <i>Making the pGal 1,10-IsPETase Plasmid</i>
+                            <h4 class="font-weight-bold custom-heading">
+                                <i>Making the pGal 1,10-IsPETase Plasmid</i>
                             </h4>
                            <img src="https://static.igem.wiki/teams/5094/experiment/making-ispetase-on-pgal-1-10-plasmid.jpg" alt="making-ispetase-on-pgal-1-10-plasmid" width="800">
-                           <p class="bigger-text">
-                            For making pGal 1,10-IsPETase, we performed similar experiments as that of making T7-IsPETase. The main difference occurs during double enzyme digestion. When performing double enzyme digestion, we used XmaI and SpeI double enzymes, in contrast to BamHI and HindIII enzymes used during double enzyme digestion for T7-IsPETase. For the rest of the procedure, the making of pGal 1,10-IsPETase is identical to that of the experiments done when making T7-IsPETase.
-                           </p>
-
-
-
-
-                       <!--Mutating the Plasmids - Site-Directed Mutagenesis -->
+                            <p class = "bigger-text">
+                                <strong>Fig.3</strong> Making pGal1,10-IsPETase plasmid diagram
+                            </p>
+                            <p class="bigger-text">
+                                For making pGal 1,10-IsPETase, we performed similar experiments as that of making T7-IsPETase. The main difference occurs during double enzyme digestion. When performing double enzyme digestion, we used XmaI and SpeI double enzymes, in contrast to BamHI and HindIII enzymes used during double enzyme digestion for T7-IsPETase. For the rest of the procedure, the making of pGal 1,10-IsPETase is identical to that of the experiments done when making T7-IsPETase.
+                            </p>
+                           
 
 
-                           <h4 class="font-weight-bold custom-heading">
-                                   <i>Mutating the Plasmids - Site-Directed Mutagenesis</i>
+                            <h4 class="font-weight-normal custom-heading">
+                                <i>Proof of Concepts</i>
                             </h4>
-                    
-                                <img src="https://static.igem.wiki/teams/5094/experiment/fig4.png" alt="fig4" width="800">
-                              
-                               <h4 class="font-weight-normal custom-heading">
-                                   <i>Amplification of mutant DNA</i>
-                               </h4>
-                                   <p class="bigger-text">
-                                    Design nucleotide mutations on the forward and reverse primers, changing IsPETase serin 121 to glutamic acid. Next, perform PCR amplification: for the PCR, prepare the T7-IsPETase a DNA template, pfu DNA polymerase buffer, pfu DNA polymerase, dNTP mix, and the mutated forward and reverse primers. The mutated plasmid will be amplified after PCR. Thus, we obtain copies of the mutated plasmid.
-                                   </p>
-
+                            <p class = "bigger-text">
+                                After our experiments, we did PCR again to confirm the yeast contained our team’s pGal1,10-IsPETase plasmid:
+                            </p>
+                        
+                        <img src = "https://static.igem.wiki/teams/5094/experiment/fig4.png" alt="fig4" width="800">
+                        <img src = "https://static.igem.wiki/teams/5094/experiment/fig5.png" alt="fig5" width="800">
+                       <!--Mutating the Plasmids - Site-Directed Mutagenesis -->
 
-                               <h4 class="font-weight-normal custom-heading">
-                                   <i>Degradation of parental DNA </i>
-                               </h4>
-                                   <p class="bigger-text">
-                                    After the PCR, we separate the mutated plasmid, T7-IsPETase<sup>S121E</sup> plasmid, from the parent plasmid by adding 1ul of DpnI to the PCR reaction at 37 degrees for 1 hour. This allows the DpnI to digest the methylation on the parental DNA, leaving only the T7-IsPETaseS121E plasmid.
-                                   </p>
-                                   <h5 class="font-weight-lighter">
-                                       <i>Proof of concept:</i>
-                                   </h5>
-                                   <img src="https://static.igem.wiki/teams/5094/experiment/fig5.png" alt="fig5" width="800">
+                           
+                       
+                        <h4 class="font-weight-bold custom-heading">
+                            <i>Mutating the Plasmids - Site-Directed Mutagenesis</i>
+                        </h4>         
+                            <img src="https://static.igem.wiki/teams/5094/experiment/site-directed-mutagenesis.jpg" alt="site-directed-mutagenesis Image" width="800">
+                                <h4 class="font-weight-normal custom-heading">
+                                    <i>Amplification of mutant DNA</i>
+                                </h4>
+                                    <p class="bigger-text">
+                                        To mutate our IsPETase, we designed point mutations on the forward and reverse primers, changing IsPETase serin 121 to glutamic acid. Next, we performed PCR amplification: for the PCR, prepare the T7-IsPETase a DNA template, pfu DNA polymerase buffer, pfu DNA polymerase, dNTP mix, and the mutated forward and reverse primers. The mutated plasmid was amplified after PCR. Thus, we obtained copies of the mutated plasmid.
+                                    </p>
+                                <h4 class="font-weight-normal custom-heading">
+                                    <i>Degradation of parental DNA </i>
+                                </h4>
+                                    <p class="bigger-text">
+                                        After the PCR, we separate the mutated plasmid, T7-IsPETase<sup>S121E</sup> plasmid, from the parent plasmid by adding 1ul of DpnI to the PCR reaction at 37 degrees for 1 hour. This allows the DpnI to digest the methylation on the parental DNA, leaving only the T7-IsPETaseS121E plasmid.
+                                    </p>
+                                <h4 class = "font-weight-normal custom-heading">
+                                    <i>Bacterial Transformation into E.coli</i>
+                                </h4>
+                                    <p class = "bigger-text">
+                                        We transformed  the mutated plasmid into DH5É‘ bacteria competent cells via 42 degrees heat shock protocol on LB-amp selection plates. Then, we prepared it for LB-AMP plate selection, and the resulting bacteria were the E. coli that contained the T7-IsPETaseS121E plasmid. By performing bacterial transformation, we obtained more single bacterial colonies that contained the T7-IsPETaseS121E plasmid.
+                                    </p>
+                                 
                           
-                               <h4 class="font-weight-normal custom-heading">
-                                   <i>Bacterial transformation into E. Coli</i>
-                               </h4>
-                                   <p class="bigger-text">
-                                    Transform the mutated plasmid into DH5<span>&#593;</span> bacteria competent cells via 42 degrees heat shock protocol on  LB-amp selection plates. Then, we can prepare it for LB-AMP plate selection, and the resulting bacteria will be the E. coli that contains the T7-IsPETaseS121E plasmid. By performing bacterial transformation, we obtain more single bacterial colonies containing the T7-IsPETaseS121E plasmid.
-                                   </p>
-
-
-                               <h4 class="font-weight-normal custom-heading">
+                              
+                                <h4 class="font-weight-normal custom-heading">
                                    <i>Inoculate bacterial colonies</i>
-                               </h4>
-                                   <p class="bigger-text">
-                                    Inoculate several bacterial colonies on LB-amp plates and broth; by doing this, we can select the colonies that have the T7-IsPETaseS121E plasmid with an amp-resistant gene. Plate the transformed bacteria on LB-AMP plates and broth. The ampicillin in the plates selects bacteria that have taken up the T7-IsPETaseS121E plasmid, as the plasmid contains an ampicillin resistance gene, killing the bacterial colonies that do not contain the plasmid. We now know our bacterial colonies contain the T7-IsPETaseS121E plasmid.
-                                   </p>
-
-
-                               <h4 class="font-weight-normal custom-heading">
-                                   <i>Bacterial plasmid extraction</i>
-                               </h4>
-                                   <p class="bigger-text">
-                                    After we get more copies of bacteria cells containing the mutated plasmid, we use the bacterial plasmid extraction protocol to extract the mutated plasmid from the bacteria cells. our team uses TENs buffer containing a more basic solution and 10% SDS to break down bacterial cell membranes and then 3M NaOAC PH5.2 is added to neutralize the solution to precipitate down protein and membrane debris. RNase is used to break down all of the RNA in the tube and incubate at 37 degrees for 20-30 mins. We then use phenol-chloroform to separate the proteins and debris from our plasmids. After extracting the top layer of the remaining mixture, we add ethanol and 3M sodium acetate to precipitate the plasmid at the bottom of the tube. During this stage, the ethanol interacts with the plasmids and helps the plasmids to precipitate at the bottom of the tube. Spin down the mixture and discard the supernatant, leaving only the pellet. Again, add ethanol to clean up the chemicals attached to the plasmids. Finally, spin down the mixture and discard the supernatant, and the pure, desired plasmid pellet will be at the bottom of the tube and resuspended with dH2O. Need to repeat two more times of the site-directed mutagenesis to get triple mutations on the IsPETase, and finally, those plasmids will be sent out for sequencing. 
-                                   </p>
-
-
-                               <h4 class="font-weight-normal custom-heading">
-                                   <i>Checking the sequence</i>
-                               </h4>
-                                   <p class="bigger-text">
-                                    After completing each site directed mutagenesis, we sent our mutant plasmids to Mission Biotech to check our mutation results.
-                                   </p>
-                       </div>
+                                </h4>
+                                    <p class="bigger-text">
+                                        Inoculate several bacterial colonies on LB-amp plates and broth; by doing this, we can select the colonies that have the T7-<i>Is</i>PETase<sup>S121E</sup> plasmid with an amp-resistant gene. Plate the transformed bacteria on LB-AMP plates and broth. The ampicillin in the plates selects bacteria that have taken up the T7-<i>Is</i>PETase<sup>S121E</sup> plasmid, as the plasmid contains an ampicillin resistance gene, killing the bacterial colonies that do not contain the plasmid. We now know our bacterial colonies contain the T7-<i>Is</i>PETase<sup>S121E</sup> plasmid.
+                                    </p>
+                                <h4 class="font-weight-normal custom-heading">
+                                    <i>Bacterial plasmid extraction</i>
+                                </h4>
+                                    <p class="bigger-text">
+                                        After we got more copies of bacteria cells containing the mutated plasmid, we used the bacterial plasmid extraction protocol to extract the mutated plasmid from the bacteria cells. Our team used TENs buffer that contained a more basic solution and 10% SDS to break down bacterial cell membranes and then 3M NaOAC PH5.2 was added to neutralize the solution to precipitate down protein and membrane debris. RNase was used to break down all of the RNA in the tube and incubate at 37 degrees for 20-30 mins. We then used phenol-chloroform and separated the proteins and debris from our plasmids. After extracting the top layer of the remaining mixture, we added ethanol and 3M sodium acetate to precipitate the plasmid at the bottom of the tube. In this stage, the ethanol interacted with the plasmids and helped the plasmids to precipitate at the bottom of the tube. We then spun down the mixture and discard the supernatant, leaving only the pellet. Again, we added ethanol to clean up the chemicals attached to the plasmids. Finally, we spun down the mixture and discard the supernatant, and the pure, desired plasmid pellet will be at the bottom of the tube and resuspended with dH2O. We repeated two more times of the site-directed mutagenesis to get triple mutations on the IsPETase, and finally, those plasmids were sent out for sequencing. 
+                                    </p>
+                                <h4 class="font-weight-normal custom-heading">
+                                    <i>Checking the sequence</i>
+                                </h4>
+                                    <p class="bigger-text">
+                                        After completing each site directed mutagenesis, we sent our mutant plasmids to Mission Biotech to check our mutation results.
+                                    </p>
+                                <h4 class="font-weight-normal custom-heading">
+                                    <i>Proof of Concept</i>
+                                </h4>
+                               <!-- <img src = " " alt = "side directed mutagenesis proof of concept" width = "800">
+                            -->
+                        </div>
 
 
-                       <!--Checking Our Products/Functional Assays-->
-                       <div id="fourth">
-                           <h2 class="font-weight-extra-normal text-7 mb-2 bigger-text">
-                               <strong class="font-weight-extra-bold">Checking Our Products/Functional Assays</strong>
-                           </h2>
+                        <!--Checking Our Products/Functional Assays-->
+                        <div id="fourth">
+                            <h2 class="font-weight-extra-normal text-7 mb-2 bigger-text">
+                                <strong class="font-weight-extra-bold">Checking Our Products/Functional Assays</strong>
+                            </h2>
                           
-                           <h4 class="font-weight-bold custom-heading">
-                               <i>RT-qPCR</i>
-                           </h4>
-                               <p class="bigger-text">
-                                After site-directed mutagenesis, the team couldn’t make any mutations in IsPETase, however, the team decided to use the pGal1,10-eGFP composite part created by the 2022 KCIS team as a control. To manipulate our team’s wild-type of the IsPETase enzyme along with the control eGFP cloned downstream of the pGal1, 10 promoter, respectively. BBa_K418008 contained pGal1,10-eGFP created by the 2022 KCIS team as a control, BBa_K…… contained BBa_K…+BBa_K..+BBa_K… (pGal1,10- IsPETase), are then transformed into wild-type Saccharomyces Yeast Strain, BY4741, respectively. 
-                               </p>
+                                <h4 class="font-weight-bold custom-heading">
+                                    <i>RT-qPCR</i>
+                                </h4>
+                                    <!--<img src = "" alt = "time course sample location" width = "800"> -->
+                                <p class="bigger-text">
+                                    After site-directed mutagenesis, the team couldn’t make any mutations in IsPETase. However, the team decided to use the pGal1,10-eGFP composite part created by the 2022 KCIS team as a control, and test if our wild-type of pGal1,10-IsPETase produces our desired enzyme. To manipulate our team’s wild-type of the IsPETase enzyme along with the control eGFP cloned downstream of the pGal1, 10 promoter, respectively, we transformed the BBa_K418008 contained pGal1,10-eGFP created by the 2022 KCIS team and the BBa_K…… contained BBa_K…+BBa_K..+BBa_K… (pGal1,10- IsPETase) into wild-type Saccharomyces Yeast Strain, BY4741. Before explaining RT-qPCR data results, our team briefly describes each cloned gene function to generate these 2 composite parts below:
+                                </p>
                                <p class="bigger-text">
                                 Before explaining RT-qPCR data results, our team briefly describes each cloned gene function to generate these 2 composite parts below:
                                </p>
                                <ol>
-                                   <li class="bigger-text">
-                                       BBa_K418008 created by the 2022 KCIS team is transformed into BY4741 to make the BY4741 containing BBa_K418008 used as a control yeast strain in our project. The purpose of using this composite part is to determine the specification. The team wants to verify the downstream gene of the pGal1,10 promoter can be induced in the presence of galactose, eGFP protein, but can’t degrade PET plastic for the co-culture experiments later on.  
-                                   </li>
-                                   <li class="bigger-text">
-                                       BBa_K containing BBa_K+BBa_K (pGal1,10-IsPETase) is transformed into BY4741 to make the BY4741 containing BBa_K…..as the experimental yeast strain in our project. BBa_K contains a wild-type of the IsPETase encodes for the PETase enzyme specifically degrading PET plastic. The team wants to verify the downstream gene of the pGal1,10 promoter can be induced in the presence of galactose, IsPETase protein. It can also degrade PET plastic for the co-culture experiments later on. 
-                                   </li>
+                                    <li class="bigger-text">
+                                        BBa_K418008 created by the 2022 KCIS team is transformed into BY4741 to make the BY4741 containing BBa_K418008 used as a control yeast strain in our project. The purpose of using this composite part is to determine the specification. The team wants to verify the downstream gene of the pGal1,10 promoter can be induced in the presence of galactose, eGFP protein, but can’t degrade PET plastic for the co-culture experiments later on.  
+                                    </li>
+                                    <li class="bigger-text">
+                                        BBa_K containing BBa_K+BBa_K (pGal1,10-IsPETase) is transformed into BY4741 to make the BY4741 containing BBa_K…..as the experimental yeast strain in our project. BBa_K contains a wild-type of the IsPETase encodes for the PETase enzyme specifically degrading PET plastic. The team wants to verify the downstream gene of the pGal1,10 promoter can be induced in the presence of galactose, IsPETase protein. It can also degrade PET plastic for the co-culture experiments later on. 
+                                    </li>
                                 </ol>
-                               <p class="bigger-text">
-                                To further verify whether our team’s composite parts are biological function, RT-qPCR technique will be operated to detect the mRNA induction of eGFP in BY4741 containing BBa_K418008 as a control, the mRNA induction of IsPETase in BY4741 containing BBa_K…as an experimental sample, via timecourse sample collection, 0min, 30min, 60min,90min, 120min in the presence of the 2%YP-galactose medium. The BY4741 contained two different composite parts, respectively, growing in 150ml of 2%YP-glucose-200ug/ml G418, until OD600 ~0.4, and then 40 ml of yeast culture medium will be taken out as 0 min as a control. Without galactose, the pGal1,10 promoter would not be induced to express downstream of genes’ mRNA, and the rest of the culture samples will be collected, respectively, at 5000rpm for 5 mins and washing the culture samples with dH2O twice to eliminate glucose. Then transferring the 2 composite parts of the yeast culture samples to 200ml of 2%YP-galactose-200ug/ml G418, our team will take out 40ml of yeast culture medium samples at different time courses in the presence of galactose (mentioned above). 
-                               </p>
-                               <img src="Figure 1" alt="" width="800">
-
+                                <p class="bigger-text">
+                                    To further verify whether our team’s composite parts are biological function, RT-qPCR technique will be operated to detect the mRNA induction of eGFP in BY4741 containing BBa_K418008 as a control, the mRNA induction of IsPETase in BY4741 containing BBa_K…as an experimental sample, via timecourse sample collection, 0min, 30min, 60min,90min, 120min in the presence of the 2%YP-galactose medium. The BY4741 contained two different composite parts, respectively, growing in 150ml of 2%YP-glucose-200ug/ml G418, until OD600 ~0.4, and then 40 ml of yeast culture medium will be taken out as 0 min as a control. Without galactose, the pGal1,10 promoter would not be induced to express downstream of genes’ mRNA, and the rest of the culture samples will be collected, respectively, at 5000rpm for 5 mins and washing the culture samples with dH2O twice to eliminate glucose. Then transferring the 2 composite parts of the yeast culture samples to 200ml of 2%YP-galactose-200ug/ml G418, our team will take out 40ml of yeast culture medium samples at different time courses in the presence of galactose (mentioned above). 
+                                </p>
+
+                                <h4 class="font-weight-bold custom-heading">
+                                    <i>SDS Gel Electrophoresis and Western Blot</i>
+                                </h4>
+                                    <!--<img src = "" alt = "" width = "800"> -->
+                                    <p class = "bigger-text">
+                                        <strong>Fig.9:</strong> IPTG Induction Experiment
+                                    </p>
+                                    <p class = "bigger-text">
+                                        Before setting up the SDS page and western blot experiments, our team will culture 50 ml of DE3BL21 bacteria cells containing T7-IsPETase and our  mutated plasmids in LB broth medium until OD~0.2. Then cell culture will be split into half (25mls) and containing 0.5mM of IPTG at 37 °C for 6 hours and the other half (25mls) will not have IPTG at 37°C for 6 hours as controls ( BBa_K2010000, 2017 paper and 2019 paper). 
+                                        <br>
+                                        To verify whether our composite parts—BBa_K containing BBa_K+ BBa_K(T7-IsPETase).., BBa_K containing BBa_+BBa_ (T7-IsPETase Thr116A).., and BBa_K containing BBa_+BBa_ (T7-IsPETaseThr116A/k259Glu), and BBa_K containing BBa_+BBa_ (T7-IsPETaseThr116A/M154Thr )—can express the proteins our team desires in DE3BL21 bacteria, the team will do the whole cell protein extraction of the DE3BL21 bacteria being induced by IPTG, via the 95-degree boiling method in protein extract lysis buffer protocol. According to the data shown on BBa_K2010000 from the Harvard 2017 team, the IsPETase protein was in the soluble condition, and the supernatants will be collected for the SDS page and Western blot. The team performed the SDS page first. We ran an 18% SDS-PAGE gel to confirm whether the whole cell extract contained all proteins, as well as to look for a stronger band of the IsPETase along with various mutants of IsPETase protein, approximately 30 kDa in the presence of IPTG.
+                                        <br>
+                                        After 18% SDS-PAGE gel data, our team will perform the western blot technique to determine the specific IsPETase protein expression. The team cloned the IsPETase gene downstream of the 6-his tag. Once the IsPETase protein is expressed, it will also contain a his tag at the N-terminal of the IsPETase, so the his-tag antibody can be used for the western blot experiment.
+                                    </p>
+                                  
+                                <h4 class="font-weight-bold custom-heading">
+                                    <i>Co-Culture Experiment</i>
+                                </h4>
+                               <!-- <img src = "" alt = "" width = "800"> -->
+                                <p class = "bigger-text">
+                                    <strong>Fig.10:</strong> Co-Culture Experiments Design
+                                </p>
+                                <p class="bigger-text">
+                                    The more direct functional assay is to co-culture the same amount of PET film with either DE3BL21 bacteria containing T7-IsPETase plasmid along with various mutations on IsPETase enzyme, respectively in the presence of ITPG to induce T7 promoter in DE3BL21 as experimental samples, lack of ITPG as controls. The team will use a Nabi machine with 240 wavelength to detect the amount of TPA product generated daily for the co-culture experiment. The same experiment will be performed with yeast containing the pGal1,10-IsPETase plasmid, along with various mutations on IsPETase, in the presence of galactose as experimental samples, in the glucose as controls (need to write more detail)
+                                </p>
 
-                           <h4 class="font-weight-bold custom-heading">
-                               <i>Western Blot</i>
-                           </h4>
-                               <p class="bigger-text">
-                                Before setting up the SDS page and western blot experiments, our team will culture 50ml of DE3BL21 bacteria cells containing T7-IsPETase and various mutation plasmids in LB broth medium until OD~0.2, respectively. Then cell culture will be split into half (25mls) and induced at 0.5mM of IPTG at 37 degrees for 6 hours and the other half (25mls) as uninduced at 37 degrees for 6 hours as controls ( BBa_K2010000, 2017 paper and 2019 paper). 
-                               </p>
-                               <p class="bigger-text">
-                                To verify whether those composite parts, BBa_K containing BBa_K+ BBa_K(T7-IsPETase).., BBa_K containing BBa_+BBa_ (T7-IsPETase Thr116A).., and BBa_K containing BBa_+BBa_ (T7-IsPETaseThr116A/k259Glu), and BBa_K containing BBa_+BBa_ (T7-IsPETaseThr116A/M154Thr ), can express the proteins our team desires in DE3BL21 bacteria, respectively, the team will do the whole cell protein extract of the DE3BL21 bacteria being induced by IPTG for the T7 promoter induction, via the 95-degree boiling method in protein extract lysis buffer protocol, according to the data shown on BBa_K2010000 from the Harvard 2017 team, the IsPETase protein was in the soluble condition, and the supernatants will be collected for the SDS page and Western blot. The team will perform an 18% SDS page first. To confirm whether the whole cell extract contained all proteins and also see a stronger band of the IsPETase along with various mutants of IsPETase protein, approximately 30 kDa in the presence of  IPTG, an 18% SDS-PAGE gel will be run.
-                               </p>
-                               <p class="bigger-text">
-                                After 18% SDS-PAGE gel data, our team will perform the western blot technique to determine the specific IsPETase protein expression. The team cloned the IsPETase gene downstream of the 6-his tag, once the IsPETase protein is expressed, it will also contain a histag at the N-terminal of the IsPETase, so the his-tag antibody will be used for the western blot 
-                               </p>
-                           <h4 class="font-weight-bold custom-heading">
-                               <i>Co-Culture Experiments</i>
-                           </h4>
-                               <p class="bigger-text">
-                                The more direct functional assay is to co-culture the same amount of PET film with either DE3BL21 bacteria containing T7-IsPETase plasmid along with various mutations on IsPETase enzyme, respectively in the presence of ITPG to induce T7 promoter in DE3BL21 as experimental samples, lack of ITPG as controls. The team will use a Nabi machine with 240 wavelength to detect the amount of TPA product generated daily for the co-culture experiment. The same experiment will be performed with yeast containing the pGal1,10-IsPETase plasmid, along with various mutations on IsPETase, in the presence of galactose as experimental samples, in the glucose as controls (need to write more detail)
-                               </p>
-
-
-                       <!--Protocols-->
-                       <div id="fifth">
-                           <h2 class="font-weight-extra-normal text-7 mb-2 bigger-text">
-                              
-                               <strong class="font-weight-extra-bold">Protocols</strong>
-                           </h2>
-                           <ul>
-                               <li>
-                                   <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/bacterial-plasmid-extraction.pdf">Bacterial Plasmid Extraction</a>
-                               </li>
-                               <li>
-                                <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/bacterial-plasmid-extraction.bacterial-transformation-heat-shock-protocol.pdf	">Bacterial Transformation Heat Shock Protocol</a>
+                        </div>
+                        <!--Protocols-->
+                        <div id="fifth">
+                            <h2 class="font-weight-extra-normal text-7 mb-2 bigger-text">
+                                <strong class="font-weight-extra-bold">Protocols</strong>
+                            </h2>
+                          
+                            <ul>
+                                <li>
+                                    <a class="button_note bigger-text" href="https://static.igem.wiki/teams/5094/protocol/bacterial-plasmid-extraction.bacterial-transformation-heat-shock-protocol.pdf	">Bacterial Transformation Heat Shock</a>
+                                </li>
+                                <li>
+                                    <a class="button_note bigger-text" href="https://static.igem.wiki/teams/5094/protocol/co-culture-protocol.pdf">Co-Culture Experiments Protocol</a>
+                                </li>
+                                <li>
+                                    <a class="button_note bigger-text" href="https://static.igem.wiki/teams/5094/protocol/gel-electrolysis.pdf">Gel Electrolysis</a>
+                                </li>
+                                <li>
+                                    <a class="button_note bigger-text" href="https://static.igem.wiki/teams/5094/protocol/neb-enzyme-digestion-protocol.pdf	">NEB Enzyme Digestion Protocol</a>
+                                </li>
+                                
+                                <li>
+                                  
+                                    <a class = "button_note bigger-text" href = "https://static.igem.wiki/teams/5094/protocol/rt-qpcr.pdf">RT-qPCR</a> 
                                 </li>
                                <li>
-                                   <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/co-culture-protocol.pdf">Co-Culture Experiments Protocol</a>
-                               </li>
-                               <li>
-                                   <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/gel-electrolysis.pdf">Gel Electrolysis</a>
-                               </li>
-                               <li>
-                                   <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/neb-enzyme-digestion-protocol.pdf	">NEB Enzyme Digestion Protocol</a>
-                               </li>
-                               <li>
-                                   <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/site-directed-mutagenesis.pdf">Site-Directed Mutagenesis</a>
+                                   <a class="button_note bigger-text " href="https://static.igem.wiki/teams/5094/protocol/site-directed-mutagenesis.pdf">Site-Directed Mutagenesis</a>
                                </li>
+                              
                                <li>
-                                   <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/t4-ligation.pdf">T4 Ligation</a>
+                                   <a class="button_note bigger-text" href="https://static.igem.wiki/teams/5094/protocol/t4-ligation.pdf">T4 Ligation</a>
                                </li>
                                <li>
-                                   <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/western-blot.pdf">Western Blot</a>
+                                   <a class="button_note bigger-text" href="https://static.igem.wiki/teams/5094/protocol/western-blot.pdf">Western Blot</a>
                                </li>
                                <li>
-                                   <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/yeast-plasmid-transformation-protocol.pdf	">Yeast Plasmid Transformation Protocol</a>
+                                   <a class="button_note bigger-text" href="https://static.igem.wiki/teams/5094/protocol/yeast-plasmid-transformation-protocol.pdf	">Yeast Plasmid Transformation Protocol</a>
                                </li>
                                <li>
-                                   <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/yeast-genomic-dna-extraction-protocol.pdf">Yeast Genomic DNA Extraction Protocol</a>
+                                   <a class="button_note bigger-text" href="https://static.igem.wiki/teams/5094/protocol/yeast-genomic-dna-extraction-protocol.pdf">Yeast Genomic DNA Extraction Protocol</a>
                                </li>
                                <li>
-                                   <a class="button_note" href="https://static.igem.wiki/teams/5094/protocol/2x-pcr-mix-protocol.pdf">2X PCR</a>
+                                   <a class="button_note bigger-text" href="https://static.igem.wiki/teams/5094/protocol/2x-pcr-mix-protocol.pdf">2X PCR Mix Protocol</a>
                                </li>
                            </ul>
-                      
-
-
-                       </div>
+                    
+                        </div>
 
 
-                       <!--ï¼·orks Cited-->
-                       <div id="sixth">
-                           <h2 class="font-weight-extra-normal text-7 mb-2 bigger-text">
-                              
-                               <strong class="font-weight-extra-bold">Works Cited</strong>
-                           </h2>
-                           <ul>
+                        <!--ï¼·orks Cited-->
+                        <div id="sixth">
+                            <h2 class="font-weight-extra-normal text-7 mb-2 bigger-text">
+                                <strong class="font-weight-extra-bold">Works Cited</strong>
+                            </h2>
+                            <ul>
                                <li>[link]</li>
                                <li>[link]</li>
                                <li>[link]</li>
                                <li>[link]</li>
-                           </ul>
-
+                            </ul>
 
-                       </div>
+                        </div>
 
 
 
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+                    <!--
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@@ -411,8 +410,10 @@
                             References will be listed here according to the proper citation style.
                         </p>
                     </div>
+                    -->
+                    
 
-                </div>
+                
             </div>
 
         </div>