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Measurement of site-specific 13C spin−lattice relaxation in a crystalline protein

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Lewandowski, Józef R., Sein, Julien, Sass, Hans Jürgen, Grzesiek, Stephan, Blackledge, Martin and Emsley, Lyndon (2010) Measurement of site-specific 13C spin−lattice relaxation in a crystalline protein. Journal of the American Chemical Society, Vol.132 (No.24). pp. 8252-8254. doi:10.1021/ja102744b ISSN 0002-7863.

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Official URL: http://dx.doi.org/10.1021/ja102744b

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Abstract

We demonstrate that it is possible to record site-specific spin-lattice relaxation rates for the majority of (13)C sites in uniformly (13)C and (15)N labeled solid proteins as a result of the slowing down of proton-driven spin diffusion at sample spinning frequencies >= 60 kHz, thus providing a series of new experimental probes for characterizing molecular dynamics in solid proteins.

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): Spin-lattice relaxation, Proteins -- Structure, Proteins -- Analysis, Nuclear magnetic resonance spectroscopy, Molecular dynamics
Journal or Publication Title: Journal of the American Chemical Society
Publisher: American Chemical Society
ISSN: 0002-7863
Official Date: 23 June 2010
Dates:
DateEvent
23 June 2010Published
Volume: Vol.132
Number: No.24
Page Range: pp. 8252-8254
DOI: 10.1021/ja102744b
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)

Data sourced from Thomson Reuters' Web of Knowledge

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