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Multidimensional solid state NMR of anisotropic interactions in peptides and proteins

J. Chem. Phys. 128, 052207 (2008); doi:10.1063/1.2834735

Published 5 February 2008

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Benjamin J. Wylie and Chad M. Rienstra
Department of Chemistry, Department of Biochemistry and Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA
Accurate determinations of chemical shift anisotropy (CSA) tensors are valuable for NMR of biological systems. In this review we describe recent developments in CSA measurement techniques and applications, particularly in the context of peptides and proteins. These techniques include goniometeric measurements of single crystals, slow magic-angle spinning studies of powder samples, and CSA recoupling under moderate to fast MAS. Experimental CSA data can be analyzed by comparison with ab initio calculations for structure determination and refinement. This approach has particularly high potential for aliphatic 13C analysis, especially Calpha tensors which are directly related to structure. Carbonyl and 15N CSA tensors demonstrate a more complex dependence upon hydrogen bonding and electrostatics, in addition to conformational dependence. The improved understanding of these tensors and the ability to measure them quantitatively provide additional opportunities for structure determination, as well as insights into dynamics. ©2008 American Institute of Physics
History: Received 13 November 2007; accepted 19 December 2007; published 5 February 2008
Permalink: http://link.aip.org/link/?JCPSA6/128/052207/1
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KEYWORDS and PACS

Keywords
PACS
  • 87.14.ef
    Peptides
  • 82.56.Pp
    NMR of chemical processes in biomolecules
  • 33.25.+k
    Nuclear resonance and relaxation in molecules
  • 31.15.A-
    Ab initio calculations (atoms and molecules)
  • YEAR: 2008

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0021-9606 (print)   1089-7690 (online)
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