Dissection of the pH Dependence of Inhibitor Binding Energetics for an Aspartic Protease: Direct Measurement of the Protonation States of the Catalytic Aspartic Acid Residues,-Reference-Cited by-同舟云学术

Dissection of the pH Dependence of Inhibitor Binding Energetics for an Aspartic Protease: Direct Measurement of the Protonation States of the Catalytic Aspartic Acid Residues,

Published:1997-12-01 Issue:51 Volume:36 Page:16166-16172
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Xie Dong¹,Gulnik Sergei¹,Collins Laura¹,Gustchina Elena¹,Suvorov Leonid¹,Erickson John W.¹

Affiliation:

1. Structural Biochemistry Program, SAIC Frederick, National Cancer Institute−Frederick Cancer Research and Development Center, Frederick, Maryland 21702-1201

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi971550l

Reference40 articles.

1. X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin

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