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Weak long-range correlated motions in a surface patch of ubiquitin involved in molecular recognition.

ABSTRACT: Long-range correlated motions in proteins are candidate mechanisms for processes that require information transfer across protein structures, such as allostery and signal transduction. However, the observation of backbone correlations between distant residues has remained elusive, and only local correlations have been revealed using residual dipolar couplings measured by NMR spectroscopy. In this work, we experimentally identified and characterized collective motions spanning four ?-strands separated by up to 15 Å in ubiquitin. The observed correlations link molecular recognition sites and result from concerted conformational changes that are in part mediated by the hydrogen-bonding network.

SUBMITTER: Fenwick RB

PROVIDER: S-EPMC3686050 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Weak long-range correlated motions in a surface patch of ubiquitin involved in molecular recognition.

Fenwick R Bryn RB Esteban-Martín Santi S Richter Barbara B Lee Donghan D Walter Korvin F A KF Milovanovic Dragomir D Becker Stefan S Lakomek Nils A NA Griesinger Christian C Salvatella Xavier X

Journal of the American Chemical Society 20110620 27

Long-range correlated motions in proteins are candidate mechanisms for processes that require information transfer across protein structures, such as allostery and signal transduction. However, the observation of backbone correlations between distant residues has remained elusive, and only local correlations have been revealed using residual dipolar couplings measured by NMR spectroscopy. In this work, we experimentally identified and characterized collective motions spanning four β-strands sepa ...[more]

PMID: 21634390

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