Methyl Rotation Barriers in Proteins from 2H Relaxation Data. Implications for Protein Structure-Reference-Cited by-同舟云学术

Methyl Rotation Barriers in Proteins from 2H Relaxation Data. Implications for Protein Structure

Published:2007-05-01 Issue:21 Volume:129 Page:6827-6838
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Xue Yi¹,Pavlova Maria S.¹,Ryabov Yaroslav E.¹,Reif Bernd¹,Skrynnikov Nikolai R.¹

Affiliation:

1. Contribution from the Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette Indiana 47907-2084, and Forschunginstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0702061

Reference81 articles.

1. Protein Side-Chain Dynamics Observed by Solution- and Solid-State NMR: Comparative Analysis of Methyl 2H Relaxation Data

2. Characterization of leucine side-chain reorientation in collagen-fibrils by solid-state 2H NMR.

3. Measurement of 2H T1 and T1.rho. Relaxation Times in Uniformly 13C-Labeled and Fractionally 2H-Labeled Proteins in Solution

4. Dynamics of methyl groups in proteins as studied by proton-detected carbon-13 NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease

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