Structural highlights
Publication Abstract from PubMed
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 beta-strands separated by up to 15 A 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.
Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition.,Fenwick RB, Esteban-Martin S, Richter B, Lee D, Walter KF, Milovanovic D, Becker S, Lakomek NA, Griesinger C, Salvatella X J Am Chem Soc. 2011 Jul 13;133(27):10336-10339. Epub 2011 Jun 20. PMID:21634390[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fenwick RB, Esteban-Martin S, Richter B, Lee D, Walter KF, Milovanovic D, Becker S, Lakomek NA, Griesinger C, Salvatella X. Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition. J Am Chem Soc. 2011 Jul 13;133(27):10336-10339. Epub 2011 Jun 20. PMID:21634390 doi:10.1021/ja200461n
