Lewandowski, Józef R., Sein, Julien, Blackledge, Martin and Emsley, Lyndon (2010) Anisotropic collective motion contributes to nuclear spin relaxation in crystalline proteins. Journal of the American Chemical Society, Vol.132 (No.4). pp. 1246-1248. doi:10.1021/ja907067j ISSN 0002-7863.

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Abstract

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 (15)N spin-lattice relaxation rates and propose that the effect of domain motions should be included in solid-state NMR analyses of protein dynamics.

Item Type:	Journal Article
Subjects:	Q Science > QC Physics Q Science > QD Chemistry
Divisions:	Faculty of Science, Engineering and Medicine > Science > Chemistry
Library of Congress Subject Headings (LCSH):	Nuclear spin, Relaxation phenomena, Proteins -- Structure, Anisotropy, Nuclear magnetic resonance spectroscopy
Journal or Publication Title:	Journal of the American Chemical Society
Publisher:	American Chemical Society
ISSN:	0002-7863
Official Date:	3 February 2010
Dates:	Date Event 3 February 2010 Published
Volume:	Vol.132
Number:	No.4
Page Range:	pp. 1246-1248
DOI:	10.1021/ja907067j
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	France. Agence nationale de la recherche (ANR), Sixth Framework Programme (European Commission) (FP6), European Union (EU)
Grant number:	RII3-026145 (FP6), PIRG03-GA-2008-231026 (EU)

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