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research article

Cross-correlated chemical shift modulation: A signature of slow internal motions in proteins

Frueh, Dominique  
•
Tolman, Joel R.
•
Bodenhausen, Geoffrey  
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2001
Journal of the American Chemical Society

A novel NMR expt. allows one to characterize slow motion in macromols. The method exploits the fact that motions, such as rotation about dihedral angles, induce correlated fluctuations of the isotropic chem. shifts of the nuclei in the vicinity. The relaxation of two-spin coherences involving Ca and Cb nuclei in proteins provides information about correlated fluctuations of the isotropic chem. shifts of Ca and Cb. The difference between the relaxation rates of double- and zero-quantum coherences C+a C+b and C+a C-b is shown to be affected by cross-correlated chem. shift modulation. In ubiquitin, evidence for slow motion is found in loops or near the ends of b-strands and a-helixes. [on SciFinder (R)]

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Type
research article
DOI
10.1021/ja003487k
Author(s)
Frueh, Dominique  
Tolman, Joel R.
Bodenhausen, Geoffrey  
Zwahlen, Catherine
Date Issued

2001

Published in
Journal of the American Chemical Society
Volume

123

Issue

20

Start page

4810

End page

4816

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LRMB  
Available on Infoscience
February 22, 2006
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/225655
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