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|a 10.1016/j.pnmrs.2014.11.001
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|a eng
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|a Torchia, Dennis A
|e verfasserin
|4 aut
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|a NMR studies of dynamic biomolecular conformational ensembles
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|c 2015
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|a Text
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|a ƒaComputermedien
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|a Date Completed 13.10.2015
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|a Date Revised 12.05.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Published by Elsevier B.V.
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|a Multidimensional heteronuclear NMR approaches can provide nearly complete sequential signal assignments of isotopically enriched biomolecules. The availability of assignments together with measurements of spin relaxation rates, residual spin interactions, J-couplings and chemical shifts provides information at atomic resolution about internal dynamics on timescales ranging from ps to ms, both in solution and in the solid state. However, due to the complexity of biomolecules, it is not possible to extract a unique atomic-resolution description of biomolecular motions even from extensive NMR data when many conformations are sampled on multiple timescales. For this reason, powerful computational approaches are increasingly applied to large NMR data sets to elucidate conformational ensembles sampled by biomolecules. In the past decade, considerable attention has been directed at an important class of biomolecules that function by binding to a wide variety of target molecules. Questions of current interest are: "Does the free biomolecule sample a conformational ensemble that encompasses the conformations found when it binds to various targets; and if so, on what time scale is the ensemble sampled?" This article reviews recent efforts to answer these questions, with a focus on comparing ensembles obtained for the same biomolecules by different investigators. A detailed comparison of results obtained is provided for three biomolecules: ubiquitin, calmodulin and the HIV-1 trans-activation response RNA
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|a Journal Article
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|a Research Support, N.I.H., Intramural
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|a Review
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|a Dynamics
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|a Order parameter
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|a Relaxation
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|a Residual dipolar coupling
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|a Spin
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|i Enthalten in
|t Progress in nuclear magnetic resonance spectroscopy
|d 1998
|g 84-85(2015) vom: 11. Feb., Seite 14-32
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|u http://dx.doi.org/10.1016/j.pnmrs.2014.11.001
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