Determining Valine Side-Chain Rotamer Conformations in Proteins from Methyl 13C Chemical Shifts: Application to the 360 kDa Half-Proteasome-Reference-Cited by-同舟云学术

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Determining Valine Side-Chain Rotamer Conformations in Proteins from Methyl 13C Chemical Shifts: Application to the 360 kDa Half-Proteasome

Published:2011-05-05 Issue:21 Volume:133 Page:8272-8281
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Hansen D. Flemming¹,Kay Lewis E.²

Affiliation:

1. Institute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower Street, London WC1E 6BT, United Kingdom

2. Departments of Molecular Genetics, Biochemistry and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja2014532

Reference56 articles.

1. Atomic-Level Characterization of the Structural Dynamics of Proteins

2. Enzyme Dynamics During Catalysis Measured by NMR Spectroscopy

3. Molecular dynamics and protein function

4. Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution

5. Solution NMR Spin Relaxation Methods for Characterizing Chemical Exchange in High-Molecular-Weight Systems

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