Conservation, Evolutionary: Difference between revisions
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Eric Martz (talk | contribs) →Conservation for Domain Folding: polishing |
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==Conservation for Domain Folding== | ==Conservation for Domain Folding== | ||
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, in order to turn back into the folded protein domain, at the protein molecular surface. Therefore, it is common to see 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, in order to turn back into the folded protein domain, at the protein molecular surface. Therefore, it is common to see highly conserved residues that enable turns, or break helices, notably '''glycines or prolines''', on protein structure surfaces. | ||
Every structure in ''Proteopedia'' has a link to be displayed in [http://firstglance.jmol.org FirstGlance in Jmol]. There, you can use the ''Find'' dialog to enter the name of an amino acid, e.g. ''glycine'' or ''proline'', and the positions of all of the specified amino acids will be highlighted. You can then visualize their distribution in the 3D structure. | Every structure in ''Proteopedia'' has a link to be displayed in [http://firstglance.jmol.org FirstGlance in Jmol]. There, you can use the ''Find'' dialog to enter the name of an amino acid, e.g. ''glycine'' or ''proline'', and the positions of all of the specified amino acids will be highlighted. You can then visualize their distribution in the 3D structure. | ||
