Alteration of Hydrogen Bonding in the Vicinity of Histidine 48 Disrupts Millisecond Motions in RNase A-Reference-Cited by-同舟云学术

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Alteration of Hydrogen Bonding in the Vicinity of Histidine 48 Disrupts Millisecond Motions in RNase A

Published:2011-02-10 Issue:10 Volume:50 Page:1723-1730
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Doucet Nicolas¹,Khirich Gennady¹,Kovrigin Evgenii L.²,Loria J. Patrick¹³

Affiliation:

1. Department of Chemistry, Yale University, New Haven, Connecticut 06520, United States

2. Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, United States

3. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi1018539

Reference33 articles.

1. Multiple Conformational Changes in Enzyme Catalysis

2. Relaxation Spectra of Ribonuclease. I. The Interaction of Ribonuclease with Cytidine 3′-Phosphate

3. Catalysis by Ribonuclease A Is Limited by the Rate of Substrate Association

4. Relaxation Spectra of Ribonuclease. III. Further Investigation of the Interaction of Ribonuclease and Cytidine 3'-Phosphate

5. Kinetic and equilibrium studies of the ribonuclease-catalyzed hydrolysis of uridine 2',3'-cyclic phosphate

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2. Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding;Biochemistry;2020-01-07

3. NMR Line Shapes in Molecular Mechanisms with Ligand Binding and Multiple Conformers;2020-01-05

4. Nucleotide substrate binding characterization in human pancreatic-type ribonucleases;PLOS ONE;2019-08-08

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