Determination of Leu Side-Chain Conformations in Excited Protein States by NMR Relaxation Dispersion-Reference-Cited by-同舟云学术

Determination of Leu Side-Chain Conformations in Excited Protein States by NMR Relaxation Dispersion

Published:2009-12-11 Issue:1 Volume:132 Page:42-43
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Hansen D. Flemming¹,Neudecker Philipp¹,Vallurupalli Pramodh¹,Mulder Frans A. A.¹,Kay Lewis E.¹

Affiliation:

1. University of Toronto, Departments of Molecular Genetics, Biochemistry and Chemistry, 1 King’s College Circle, Toronto, M5S 1A8, ON, Canada, and Groningen Biomolecular Sciences and Biotechnology Institute, 9747 AG Groningen, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja909294n

Reference22 articles.

1. Nuclear Magnetic Resonance Methods for Quantifying Microsecond-to-Millisecond Motions in Biological Macromolecules

2. The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis

3. Intrinsic dynamics of an enzyme underlies catalysis

4. Binding Kinetics of Histone Chaperone Chz1 and Variant Histone H2A.Z-H2B by Relaxation Dispersion NMR Spectroscopy

5. Measurement of Slow (μs−ms) Time Scale Dynamics in Protein Side Chains by 15N Relaxation Dispersion NMR Spectroscopy: Application to Asn and Gln Residues in a Cavity Mutant of T4 Lysozyme

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