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Functional significance of flexibility in proteins
Author(s) -
Huber Robert,
Bennett William S.
Publication year - 1983
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360220136
Subject(s) - chemistry , trypsinogen , trypsin , flexibility (engineering) , biochemistry , enzyme , antibody , computational biology , immunology , biology , statistics , mathematics
Abstract The structural basis and the functional implications of large‐scale flexibility are discussed for three systems: trypsin–trypsinogen, immunoglobulins, and citrate synthase. The trypsin–trypsinogen system provides an example in which an order–disorder transition is used as a means to regulate enzymatic activity. Immunoglobulins demonstrate how flexibly linked domains may be used to allow the binding of ligands with diverse arrangements. In citrate synthase, domain motion forms an active site that is shielded from solvent. Analogous large‐scale flexibility has been observed in a number of other systems.