Relation between native ensembles and experimental structures of proteins.

Abstract:

:Different experimental structures of the same protein or of proteins with high sequence similarity contain many small variations. Here we construct ensembles of "high-sequence similarity Protein Data Bank" (HSP) structures and consider the extent to which such ensembles represent the structural heterogeneity of the native state in solution. We find that different NMR measurements probing structure and dynamics of given proteins in solution, including order parameters, scalar couplings, and residual dipolar couplings, are remarkably well reproduced by their respective high-sequence similarity Protein Data Bank ensembles; moreover, we show that the effects of uncertainties in structure determination are insufficient to explain the results. These results highlight the importance of accounting for native-state protein dynamics in making comparisons with ensemble-averaged experimental data and suggest that even a modest number of structures of a protein determined under different conditions, or with small variations in sequence, capture a representative subset of the true native-state ensemble.

authors

Best RB,Lindorff-Larsen K,DePristo MA,Vendruscolo M

doi

10.1073/pnas.0511156103

subject

Has Abstract

pub_date

2006-07-18 00:00:00

pages

10901-6

issue

29

eissn

0027-8424

issn

1091-6490

pii

0511156103

journal_volume

103

pub_type

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