diff --git a/wiki/pages/engineering-design2.html b/wiki/pages/engineering-design2.html
index e9765d875c8517834e4ce2e60540073b15d12274..c3ef17d40f3e18fd41d7faae24c3f27ecf2e9b8b 100644
--- a/wiki/pages/engineering-design2.html
+++ b/wiki/pages/engineering-design2.html
@@ -18,10 +18,13 @@ Engineering Cycle  - And we go again… Design- Build- Test
     <p>
     <b> And we go again…Design- Build- Test </b><br>
 
-For the next set of experiments, we decided to order the mutants of cspF (just nine nucleotides in length) and see if they could sufficiently upregulate or downregulate expression levels. For this purpose, we decided to make single-point substitution mutations in the sequence of cspF. This generated a library of 27 potential sequences of UTRs to test. However, we decided to pick only ten sequences to start. To make this choice, we predicted the expression of all sequences in OSTIR with the pre-start codon cut-off set to 38 and the post-start codon cut-off set to 35. After ranking all 26 mutants (one of them was an illegal sequence) in decreasing order of predicted expression, we chose ten evenly spaced mutants from this set. In the earlier batch, we had ordered Promoter-UTR BioBricks. We realized that it would be much faster and more convenient to order the forward and reverse “mega-primers” with a single nucleotide mismatch and create the entire plasmid using PCR from the existing cspF plasmids. In this iteration, we plan to take the readings in the log phase as well as the stationary phase as suggested by <a href="{{ url_for('pages', page='human-practices9') }}"> Prof Cameron</a>. We have also done project <a href="{{ url_for('pages', page='model') }}">Modelling</a> using neural networks to make an attempt to correlate the expression values we specifically obtain in this iteration of engineering cycle to our own model. We have already predicted the expression of these nucleotides in Salis' RBS calculator version 2 and OSTIR and through our neural network which we trained on the basis of the data available in literature. The details of this are given on the Project Modelling Page.<br></p><p>
-We tested these sequences out. Just a day before the Wiki Freeze we received our results and wish to incorporate the data. The basic analysis suggests that there was not much of a variation in the F/OD values. This suggests that probably in some cases, changing just one nucleotide does not change the expression. This may have structural correlations. We have correlated it with NuPACK. However, while calculating the relative performance with respect to cspF, we realised that if a G/C in the original sequence GGAATTTTT was changed to an A/T then the F/OD values went lower. Whereas, if the vice versa was done, the F/OD value increased. We already have an experimentally validated library that gives a range of expression with respect to just the RBS. Our further designs will be based in learnings and developments from this experiment. We wish to modify the GC content of cspF by making multiple mutations in one sequence while maintaining its structural scaffold in the third engineering cycle. The next aspect that we wish to check is that keeping the structural scaffold of the cspF intact we wish to add additional structural complexities of different levels to it through our sequence and see how the gene expression changes. <br>
-As mentioned we finished the testing aspect of our second engineering cycle just recently, hence we are still to come up with the sequences and design for the third cycle. A part of the second engineering cycle was to test the truncated UTRs as well from the previous 16 UTRs which is still in process.<br>
-      </p>
+For the next set of experiments, we ordered the mutants of cspF (just nine nucleotides in length) to see if they could sufficiently upregulate or downregulate expression levels. For this purpose, we decided to make single-point substitution mutations in the sequence of cspF. The ordered sequences are referred to as SDM (Site-Directed Mutant), and the parts are also named in this fashion. <br></p><p>
+
+<br><p>This generated a library of 27 potential sequences of UTRs to test. However, we decided to pick only 10 sequences to start. To make this choice, we predicted the expression of all sequences in OSTIR with the pre-start codon cut-off set to 38 and the post-start codon cut-off set to 35. After ranking 26 mutants (one of them was an illegal sequence) in decreasing order of predicted expression, we chose ten evenly spaced mutants from this set. In the earlier batch, we had ordered Promoter-UTR (pUTR) BioBricks. We realised that it would be much faster and more convenient to order the forward and reverse "mega-primers" with a single nucleotide mismatch and create the entire plasmid using PCR from the existing cspF plasmids. In this iteration, we also took the readings in the log and stationary phases, as suggested by <a href="{{ url_for('pages', page='human-practices9') }}"> Prof Cameron</a>. <br></p><p>
+
+We have also done project <a href="{{ url_for('pages', page='model') }}">Modelling</a> using neural networks to make an attempt to correlate the expression values we specifically obtain in this iteration of engineering cycle to our own model. We have already predicted the expression of these nucleotides in Salis' RBS calculator version 2 and OSTIR and through our neural network which we trained on the basis of the data available in literature. The details of this are given on the Project Modelling Page.<br></p>
+
+<br>
       <p>
         Following is the list of CspF mutants we designed, built oligos for and ordered:
         <br>
@@ -173,6 +176,10 @@ As mentioned we finished the testing aspect of our second engineering cycle just
         </p>
 
         <br><br>
+        <p>
+
+        </p><br>
+        <p> We tested these sequences out in two strains of E. coli: Dh5alpha, a cloning strain and BL21(DE3), an expression strain. The analysis suggests that there is not much of a variation in the F/OD values. This suggests that probably in some cases, changing just one nucleotide does not change the expression. This may have structural correlations. <br></p>
         <br>
         <p><h3>Characterization of CspF Mutants in DH5alpha Strain:</h3</p>
         <center><iframe src="https://static.igem.wiki/teams/4303/wiki/data-for-the-sdm-utrs-in-dh5alpha.pdf" width="100%" height="500px"></iframe></center> </p>
@@ -189,13 +196,16 @@ As mentioned we finished the testing aspect of our second engineering cycle just
         <p><h3>NUPACK CspF Mutants</h3</p>
         <center><iframe src="https://static.igem.wiki/teams/4303/wiki/nupack-cspf-mutants.pdf" width="100%" height="500px"></iframe></center>
         <br>
+        <p> We tested these sequences out in two strains of E. coli: Dh5alpha, a cloning strain and BL21(DE3), an expression strain. The analysis suggests that there is not much of a variation in the F/OD values. This suggests that probably in some cases, changing just one nucleotide does not change the expression. This may have structural correlations. <br></p>
+        <p> We have correlated it with NuPACK. However, while calculating the relative performance with respect to cspF, we realised that if a G/C in the original sequence GGAATTTTT was changed to an A/T then the F/OD values went lower. Whereas, if the vice versa was done, the F/OD value increased. We already have an experimentally validated library that gives a range of expression with respect to just the RBS (negative control). Our further designs will be based in learnings and developments from this experiment. <br></p>
         <p><h3>NUPACK ANALYSIS</h3></p>
         <p><ul><li>From this, the least performing UTR SDM23 clearly has a very different structure. SDM10 has a similar structure but an Relative Performance 0.21 times higher than SDM23. This could be probably because of the GC content of it being different?</li><li>
 SDM27 has the best expression and Relative Performance of 1.3. It’s structure is very different from the other UTRs. We need to perform 3D corrations.</li><li>
 SDM26 and 9 have similar structures and similar Relative Performances.</li><li>
 SDM3 and SDM5 have a similar structure and a similar Relative Performance.</li></ul>
 </p>
-        
+<br><br>
+<p>We wish to modify the GC content of cspF by making multiple mutations in one sequence while maintaining its structural scaffold in the third engineering cycle. The next aspect that we wish to check is that keeping the structural scaffold of the cspF intact we wish to add additional structural complexities of different levels to it through our sequence and see how the gene expression changes.<br></p>
   </div>
 </div>