I have conducted molecular docking simulations using AutoDock 4, and have analyzed the polar interactions between amino acid residues and the ligand. The residue information and measurements have been obtained in Armstrong units. What techniques can be employed to infer the functional importance of a particular residue in the protein's activity?
You can start with very simple residue conservation analysis in this species, its genus, family, etc by multiple sequence alignments. Residues that are very conserved usually have an important role. And by "important" I don't mean only function. It could be important for folding, regulation, etc. For more sophisticate methods, check those and more recent papers:
Predicting functionally important residues from sequence conservation
https://academic.oup.com/bioinformatics/article/23/15/1875/203579
Prediction of protein functional residues from sequence by probability density estimation
https://academic.oup.com/bioinformatics/article/24/5/613/200952
Hello Renault I hope your well:).
You can try substituting this residue with another residue and then re-measure the ligand-docking energy if pivotal in this way and or visually then inspect the protein to determine its significance i.e. compaction etc..
Thank you to all for your invaluable contributions. I really appreciate your hard work and dedication!
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