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Liaison amid disorder: non-native interactions may underpin long-range coupling in proteins.

ABSTRACT: A lattice-model study of double-mutant cycles published in BMC Structural Biology underscores how interactions in non-native conformations can lead to thermodynamic coupling between distant residues in globular proteins, adding to recent advances in delineating the often crucial roles played by disordered conformational ensembles in protein behavior.

SUBMITTER: Chan HS 

PROVIDER: S-EPMC2689430 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature

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Liaison amid disorder: non-native interactions may underpin long-range coupling in proteins.

Chan Hue Sun HS   Zhang Zhuqing Z  

Journal of biology 20090313 3

A lattice-model study of double-mutant cycles published in BMC Structural Biology underscores how interactions in non-native conformations can lead to thermodynamic coupling between distant residues in globular proteins, adding to recent advances in delineating the often crucial roles played by disordered conformational ensembles in protein behavior. ...[more]