Relaxation of Two-Spin Coherence Due to Cross-Correlated Fluctuations of Dipole−Dipole Couplings and Anisotropic Shifts in NMR of 15N,13C-Labeled Biomolecules-Reference-Cited by-同舟云学术

Relaxation of Two-Spin Coherence Due to Cross-Correlated Fluctuations of Dipole−Dipole Couplings and Anisotropic Shifts in NMR of 15N,13C-Labeled Biomolecules

Published:1999-07-01 Issue:29 Volume:121 Page:6876-6883
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Chiarparin Elisabetta¹,Pelupessy Philippe¹,Ghose Ranajeet¹,Bodenhausen Geoffrey¹

Affiliation:

1. Contribution from the Section de Chimie, Université de Lausanne, BCH, 1015 Lausanne, Switzerland, and Département de chimie, associé au CNRS, Ecole Normale Supérieure, 24 rue Lhomond, 75231 Paris Cedex 05, France

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja984390p

Reference29 articles.

1. Protein Backbone Dynamics and 15N Chemical Shift Anisotropy from Quantitative Measurement of Relaxation Interference Effects

2. Cross-correlation effects in the transverse relaxation of multiple-quantum transitions of heteronuclear spin systems

3. Quantitative Measurement of Relaxation Interference Effects between 1HN CSA and 1H−15N Dipolar Interaction: Correlation with Secondary Structure

4. Experimental Characterization of Models for Backbone Picosecond Dynamics in Proteins. Quantification of NMR Auto- and Cross-correlation Relaxation Mechanisms Involving Different Nuclei of the Peptide Plane

5. A study of protein side-chain dynamics from new 2 H auto-correlation and 13 C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk 1 1Edited by P. E. Wright

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