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- W4239586283 abstract "Induced-fit configurational transitions in proteins can take many forms. In cases, we find small “closures” of a loop onto the substrate. In other cases, the structural changes triggered by a ligand involve large rearrangements that affect entire domains. The nature of these transitions is normally assessed by a visual analysis or in terms of simple local geometrical parameters, such as interresidue distances, backbone dihedral angles, and relative displacements between domains. This approach is limited and rather undiscriminating. In this work, we apply recently introduced ideas from macromolecular shape analysis to characterize the global shape changes accompanying “open closed” transitions in proteins. Here, we monitor two distinct properties simultaneously: molecular size and self-entanglements. The method is applied to some proteins exhibiting pairs of structurally different conformations (adenylate kinase, hexokinase, citrate synthase, alcohol dehydrogenase, triosephosphate isomerase, thioredoxin, and aspartate amino-transferase). The conformational change associated with these proteins is classified according to an order parameter that considers various molecular shape features. The results allow one to recognize, in a nonvisual fashion, the likely occurrence of local or global structural rearrangements. In addition, the technique provides an insight into folding features that may remain invariant during the configurational transitions. © 1996 John Wiley & Sons, Inc." @default.
- W4239586283 created "2022-05-12" @default.
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- W4239586283 date "1996-11-01" @default.
- W4239586283 modified "2023-09-26" @default.
- W4239586283 title "Characterization of global molecular shape transitions between “open” and “closed” protein conformations" @default.
- W4239586283 doi "https://doi.org/10.1002/(sici)1097-0282(199611)39:5<671::aid-bip6>3.3.co;2-p" @default.
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