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Functional protein domains from the thermally driven motion of polypeptide chains: A proposal
Author(s) -
Hoh Jan H.
Publication year - 1998
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(19980801)32:2<223::aid-prot8>3.0.co;2-l
Subject(s) - polypeptide chain , protein structure , range (aeronautics) , bristle , biophysics , biological system , chemistry , crystallography , statistical physics , physics , computational biology , biology , materials science , biochemistry , amino acid , composite material , brush
It is proposed that the thermally driven motion of certain polypeptide chains, including those that are part of an otherwise stable folded protein, produces time‐averaged three‐dimensional domains that confer unique functions to a protein. These domains may be controlled by collapsing the polypeptide into an enthalpically favored structure, or extending it into an entropically dominated form. In the extended form, these domains occupy a relatively large space, which may be used to regulate protein–protein interactions and confer mechanical properties to proteins. This “entropic bristle” model makes several predictions about the structure and properties of these domains, and the predictions are used to reevaluate a range of biophysical studies on proteins. The outcome of the analysis suggests that the entropic bristle can be used to explain a wide range of disparate and apparently unrelated experimental observations. Proteins 32:223–228, 1998. © 1998 Wiley‐Liss, Inc.