Conservation, Evolutionary: Difference between revisions
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Certain residues on the surfaces of protein molecules tend to be conserved in order to maintain proper folding, rather than because they are part of a site functioning to interact with substrate, ligand, or a protein partner. Secondary structure elements need to break at the protein molecular surface in order to turn back into the folded protein domain. Therefore, it is common to see isolated highly conserved residues that enable turns, or break helices, notably '''glycines or prolines''', on protein structure surfaces. | Certain residues on the surfaces of protein molecules tend to be conserved in order to maintain proper folding, rather than because they are part of a site functioning to interact with substrate, ligand, or a protein partner. Secondary structure elements need to break at the protein molecular surface in order to turn back into the folded protein domain. Therefore, it is common to see isolated highly conserved residues that enable turns, or break helices, notably '''glycines or prolines''', on protein structure surfaces. | ||
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]]. | ||
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. | ||
