Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 4, Pages 1246-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja907067j
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Funding
- Agence National de la Recherche
- EC [RII3-026145, EU-NMR]
- EU Marie Curie IRG Fellowship [PIRG03-GA-2008-231026]
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A model for calculating the influence of anisotropic collective motions on NMR relaxation rates in crystalline proteins is presented. We show that small-amplitude (<10 degrees) fluctuations may lead to substantial contributions to the N-15 spin-lattice relaxation rates and propose that the effect of domain motions should be included in solid-state NMR analyses of protein dynamics.
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