Conservation, Evolutionary: Difference between revisions
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Charged residues are usually on the surfaces of folded proteins. If you see a highly conserved charged residue (''Arg, Asp, Glu, Lys''') on the surface, often it participates in a [[Salt bridges|salt bridge]]. Salt bridges help to stabilize protein folds, and hence the residues involved are often highly conserved. Example: Asp6 with Arg8 in [[1qdq]]. | Charged residues are usually on the surfaces of folded proteins. If you see a highly conserved charged residue (''Arg, Asp, Glu, Lys''') on the surface, often it participates in a [[Salt bridges|salt bridge]]. Salt bridges help to stabilize protein folds, and hence the residues involved are often highly conserved. Example: Asp6 with Arg8 in [[1qdq]]. | ||
For other situation where conservation is expected, see [[Introduction_to_Evolutionary_Conservation#Expected_vs._Unexpected_Conservation|Expected vs. Unexpected Conservation]]. | |||
Remember that you can touch any residue with the mouse in the ''Evolutionary Conservation'' scene in Proteopedia (in Jmol), and its identity will be displayed after a few seconds. This works best with spinning turned off. | Remember that you can touch any residue with the mouse in the ''Evolutionary Conservation'' scene in Proteopedia (in Jmol), and its identity will be displayed after a few seconds. This works best with spinning turned off. | ||
