Structural and Mechanistic Insight into the Inhibition of Aspartic Proteases by a Slow-Tight Binding Inhibitor from an Extremophilic Bacillus sp.: Correlation of the Kinetic Parameters with the Inhibitor Induced Conformational Changes-Reference-Cited by-同舟云学术

Structural and Mechanistic Insight into the Inhibition of Aspartic Proteases by a Slow-Tight Binding Inhibitor from an Extremophilic Bacillus sp.: Correlation of the Kinetic Parameters with the Inhibitor Induced Conformational Changes

Published:2001-08-29 Issue:38 Volume:40 Page:11525-11532
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Dash Chandravanu¹,Phadtare Sangita¹,Deshpande Vasanti¹,Rao Mala¹

Affiliation:

1. Division of Biochemical Sciences, National Chemical Laboratory, Pune 411 008, India

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi010594y

Reference45 articles.

1. The Structure and Function of the Aspartic Proteinases

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