Subangstrom Crystallography Reveals that Short Ionic Hydrogen Bonds, and Not a His-Asp Low-Barrier Hydrogen Bond, Stabilize the Transition State in Serine Protease Catalysis-Reference-Cited by-同舟云学术

Subangstrom Crystallography Reveals that Short Ionic Hydrogen Bonds, and Not a His-Asp Low-Barrier Hydrogen Bond, Stabilize the Transition State in Serine Protease Catalysis

Published:2006-06-27 Issue:28 Volume:128 Page:9086-9102
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Fuhrmann Cynthia N.¹,Daugherty Matthew D.¹,Agard David A.¹

Affiliation:

1. Contribution from the Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, 600 16th Street, Box 2240, San Francisco, California 94143-2240

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja057721o

Reference94 articles.

1. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

2. The 0.83Å Resolution Crystal Structure of α-Lytic Protease Reveals the Detailed Structure of the Active Site and Identifies a Source of Conformational Strain

3. The Low Barrier Hydrogen Bond in Enzymatic Catalysis

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