Quantitative measurement of cross-correlations between 15N and 13CO chemical shift anisotropy relaxation mechanisms by multiple quantum NMR

Pellecchia, Maurizio ; Pang, Yuxi ; Wang, Lincong ; Kurochkin, Alexander V. ; Anil Kumar, ; Zuiderweg, Erik R. P. (1999) Quantitative measurement of cross-correlations between 15N and 13CO chemical shift anisotropy relaxation mechanisms by multiple quantum NMR Journal of the American Chemical Society, 121 (39). pp. 9165-9170. ISSN 0002-7863

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Official URL: http://pubs.acs.org/doi/abs/10.1021/ja991155d

Related URL: http://dx.doi.org/10.1021/ja991155d

Abstract

This paper describes an experiment that allows the quantitative measurement of the CSA-CSA cross-correlation between backbone 15N and 13CO nuclei in uniformly enriched proteins. The CSA-CSA cross-correlation is obtained from the cross-peak intensity ratios of the double- and the zero-quantum components observed with a modified triple-quantum 2D CT-HNCO experiment. In addition, the 1HN̲15N/1HN̲13CO dipole-dipole cross-correlation was measured without relying on resolved scalar couplings using a complementary quantum 2D CT-HNCO experiment. The cross-correlation rates measured for the protein binase (12.3 kDa) were obtained with high precision but show a surprisingly large range of values. Calculations show that this range is at least partially caused by dynamical processes. The potential use of this information to characterize internal anisotropic motion is discussed.

Item Type:Article
Source:Copyright of this article belongs to American Chemical Society.
ID Code:72685
Deposited On:29 Nov 2011 03:57
Last Modified:29 Nov 2011 03:57

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