Propagating conformational changes over long (and short) distances in proteins.

Abstract:

:The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetics of the pathway between these states is also selected so that the energy of ligand binding and the speed of the transition between conformational states are physiologically appropriate. The crystallographic data of a wild-type aspartate receptor that has negative cooperativity and a mutant that has no cooperativity but has native transmembrane signaling are shown to support this model.

authors

Yu EW,Koshland DE Jr

doi

10.1073/pnas.161239298

keywords:

subject

Has Abstract

pub_date

2001-08-14 00:00:00

pages

9517-20

issue

17

eissn

0027-8424

issn

1091-6490

pii

98/17/9517

journal_volume

98

pub_type

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