Corrigendum: Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion
نویسندگان
چکیده
منابع مشابه
Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics.
Analyses of solution (15)N relaxation data and solid-state (1)H(N)-(15)N dipolar couplings from a small globular protein, alpha-spectrin SH3 domain, produce a surprisingly similar pattern of order parameters. This result suggests that there is little or no ns-mus dynamics throughout most of the sequence and, in particular, in the structured portion of the backbone. At the same time, evidence of...
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Aseries of uni- and multidimensional variants of the dipolar exchange-assisted recoupling (DEAR) NMR experiment is described and applied to determinations of (13)C-(14)N dipolar local field spectra in amino acids and dipeptides. The DEAR protocol recouples nearby nuclei by relying on differences in their relative rates of longitudinal relaxation, and has the potential to give quantitative geome...
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In this paper, we seek to compare the internal dynamics of a small globular protein, SH3 domain from alpha-spectrin, in solution and in a crystalline state. The comparison involves side-chain methyl 13C R1 relaxation rates that are highly sensitive to local dynamics in the vicinity of the methyl site. To conduct the relaxation measurements, protein samples have been prepared using specially lab...
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One-bond backbone dipolar couplings can readily be measured for proteins dissolved in a dilute liquid crystalline phase.1-3 They can be used to refine NMR structures determined by conventional methods or, in favorable cases, be sufficient to determine a structure de novo.4,5 They also provide an invaluable tool for quality evaluation.6,7 Nearly all focus thus far has been on the measurement of ...
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ژورنال
عنوان ژورنال: Angewandte Chemie International Edition
سال: 2012
ISSN: 1433-7851
DOI: 10.1002/anie.201206663