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Measurement of Cross Correlation between Dipolar Coupling and Chemical Shift Anisotropy in the Spin Relaxation of13C,15N-Labeled Proteins

✍ Scribed by Ranajeet Ghose; Kai Huang; James H Prestegard

Publisher: Elsevier Science
Year: 1998
Tongue: English
Weight: 259 KB
Volume: 135
Category: Article
ISSN: 1090-7807
DOI: 10.1006/jmre.1998.1602

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✦ Synopsis

We present a simple method for extracting interference effects between chemical shift anisotropy (CSA) and dipolar coupling from spin relaxation measurements in macromolecules, and we apply this method to extracting cross-correlation rates involving interference of amide 15N CSA and 15N-1H dipolar coupling and interference of carbonyl 13C' CSA and 15N-13C' dipolar coupling, in a small protein. A theoretical basis for the interpretation of these rates is presented. While it proves difficult to quantitatively separate the structural and dynamic contributions to these cross-correlation rates in the presence of anisotropic overall tumbling and a nonaxially symmetric chemical shift tensor, some useful qualitative correlations of data with protein structure can be seen when simplifying assumptions are made.

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