Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 131, Issue 41, Pages 14610-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja905340s
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Funding
- NSF [MCB-0918362]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0918362] Funding Source: National Science Foundation
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Correlated internal dynamics of proteins, which is believed to be important for their function, is analyzed at unprecedented precision using explicit-solvent submicrosecond molecular dynamics simulations of ubiquitin and calbindin D-9k. Without exception, all of the mobile dihedral angle pairs in ubiquitin with sizable dynamics correlations (R-2 >= 0.1) are at short-range distance. In rare cases, they involve sequentially remote dihedral angles that form sparse clusters, suggesting a structural-dynamic propagation mechanism via soft torsional couplings that act over short distances with a rapid loss of coherence over longer distances.
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