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Chevelkov, V.* ; Xue, Y.* ; Linser, R.* ; Skrynnikov, N.R.* ; Reif, B.*

Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics.

J. Am. Chem. Soc. 132, 5015-5017 (2010)
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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 ns-mus motions is found in the flexible loops and termini. These findings, corroborated by the MD simulations of alpha-spectrin SH3 in a hydrated crystalline environment and in solution, are consistent with the picture of protein dynamics that has recently emerged from the solution studies employing residual dipolar couplings.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
ISSN (print) / ISBN 0002-7863
e-ISSN 1520-5126
Quellenangaben Band: 132, Heft: 14, Seiten: 5015-5017 Artikelnummer: , Supplement: ,
Verlag American Chemical Society (ACS)
Begutachtungsstatus Peer reviewed