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231225s2017 xx |||||o 00| ||eng c |
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|a 10.1016/j.pnmrs.2017.02.001
|2 doi
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|a DE-627
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|a eng
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|a Vugmeyster, Liliya
|e verfasserin
|4 aut
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|a Static solid-state 2H NMR methods in studies of protein side-chain dynamics
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|c 2017
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 12.04.2018
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|a Date Revised 12.11.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2017 Elsevier B.V. All rights reserved.
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|a In this review, we discuss the experimental static deuteron NMR techniques and computational approaches most useful for the investigation of side-chain dynamics in protein systems. Focus is placed on the interpretation of line shape and relaxation data within the framework of motional modeling. We consider both jump and diffusion models and apply them to uncover glassy behaviors, conformational exchange and dynamical transitions in proteins. Applications are chosen from globular and membrane proteins, amyloid fibrils, peptide adsorbed on surfaces and proteins specific to connective tissues
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|a Journal Article
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|a Research Support, N.I.H., Extramural
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Review
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|a Dynamical transitions
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|a Protein dynamics
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|a Solid-state NMR
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|a Static deuteron NMR
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|a Peptides
|2 NLM
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|a Proteins
|2 NLM
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|a Deuterium
|2 NLM
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|a AR09D82C7G
|2 NLM
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|a Ostrovsky, Dmitry
|e verfasserin
|4 aut
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|i Enthalten in
|t Progress in nuclear magnetic resonance spectroscopy
|d 1998
|g 101(2017) vom: 28. Aug., Seite 1-17
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|x 1873-3301
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|g volume:101
|g year:2017
|g day:28
|g month:08
|g pages:1-17
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|u http://dx.doi.org/10.1016/j.pnmrs.2017.02.001
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