Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition
Journal of the American Chemical SocietyPublished 3 June 2011Open access
R. Bryn Fenwick, Santi Esteban-Martín, Barbara Richter, Donghan Lee, Korvin F. A. Walter, Dragomir Milovanović
Citations184
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TL;DR
This work experimentally identified and characterized collective motions spanning four β-strands separated by up to 15 Å in ubiquitin and observed correlations link molecular recognition sites and result from concerted conformational changes that are in part mediated by the hydrogen-bonding network.
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 β-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.
Keywords
ChemistryBiochemistry, Genetics and Molecular Biology
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