Protein Side-Chain Dynamics As Observed by Solution- and Solid-State NMR Spectroscopy: A Similarity Revealed-Reference-Cited by-同舟云学术

Protein Side-Chain Dynamics As Observed by Solution- and Solid-State NMR Spectroscopy: A Similarity Revealed

Published:2008-11-17 Issue:49 Volume:130 Page:16611-16621
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Agarwal Vipin¹,Xue Yi¹,Reif Bernd¹,Skrynnikov Nikolai R.¹

Affiliation:

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

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja804275p

Reference129 articles.

1. Determination of φ and χ1 Angles in Proteins from 13C−13C Three-Bond J Couplings Measured by Three-Dimensional Heteronuclear NMR. How Planar Is the Peptide Bond?

2. Weak alignment offers new NMR opportunities to study protein structure and dynamics

3. Correlation of IR spectroscopic, heat capacity, diamagnetic susceptibility and enzymatic measurements on lysozyme powder

4. Crystal structure of the stromelysin catalytic domain at 2.0 Å resolution: inhibitor-induced conformational changes 1 1Edited by R. Huber

5. Effects of temperature on protein structure and dynamics: x-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320K

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