Last modified 5th.July '95

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This section is largely based on the excellent review by Gerstein et al. (1994). Mark Gerstein is also largely responsible for The Protein Motions Database

Protein flexibility is demonstrated by large relative movements of domains, for example, in aspartic proteinases the two lobes have large relative shifts as identified by Sali et al., (1992). Such motions are important for functions like catalysis, ligand binding, regulation of activity, formation of protein assemblies and transport of metabolites. Often the domains constitute a binding site at the interface wherein closed conformations of domains correspond to inactive form of the enzyme while open conformations of domains correspond to the active form of the enzyme, illustrating induced fit in recognition (Koshland, 1958).

Mechansisms of domain movements -