Difference between revisions of "Task 6: Protein structure prediction from evolutionary sequence variation"
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Revision as of 18:38, 22 August 2013
Results
Contact Prediction
<figure id="ras_score_dist">
</figure>
<figtable id="hfe_score_dist" align="right">
</figtable>
<figure id="cm_1a6z">
</figure> <figure id="cm_hras">
</figure>
- Why are the scores of residues close in sequence amongst the highest? Why are the pairs distant in sequence (n>5) more interesting for structure prediction?
- Look at the values, range and distribution of scores.
- How many of the high-scoring pairs are true or false positives? Does this correlate with the value of the score? Visualize the predicted contacts together with the crystal structure contacts in a contact map plot.
- Can you determine evolutionary hot spots, i.e. functionally important residues? Compare to conserved sites in the MSA. Compare with your results from task 7 (when you are working on task 7, i.e. this is a task for the future).
- Here, the DI score is given. Compare the top 50 DI and CN (from freecontact) scores. How large is the overlap (>80%)?
MHC EVFOLD: constraints: 70(40%) 113(65%) 174(100%)
imm EVFOLD
RAS EVFOLD:
189 / 160
189:
76 (40%)
123 (65%)
189