Quantitative Analysis of Conformational Exchange Contributions to 1H−15N Multiple-Quantum Relaxation Using Field-Dependent Measurements. Time Scale and Structural Characterization of Exchange in a Calmodulin C-Terminal Domain Mutant-Reference-Cited by-同舟云学术

Quantitative Analysis of Conformational Exchange Contributions to 1H−15N Multiple-Quantum Relaxation Using Field-Dependent Measurements. Time Scale and Structural Characterization of Exchange in a Calmodulin C-Terminal Domain Mutant

Published:2003-12-30 Issue:3 Volume:126 Page:928-935
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lundström Patrik¹,Akke Mikael¹

Affiliation:

1. Contribution from the Department of Biophysical Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja037529r

Reference53 articles.

1. New techniques in structural NMR — anisotropic interactions

2. Characterizing Protein-Protein Complexes and Oligomers by Nuclear Magnetic Resonance Spectroscopy

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