Dissection of Binding Energy with Native and Ligand-Bound Protein Stabilities: Determining the Affinity of Ultratight-Binding Inhibitors of HIV-1 Protease and Its Drug-Resistance Mutants-Reference-Cited by-同舟云学术

Dissection of Binding Energy with Native and Ligand-Bound Protein Stabilities: Determining the Affinity of Ultratight-Binding Inhibitors of HIV-1 Protease and Its Drug-Resistance Mutants

Published:2000-11-03 Issue:46 Volume:122 Page:11533-11534
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Xie Dong¹,Gulnik Sergei¹,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

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja003230m

Reference11 articles.

1. Kinetic Characterization and Cross-Resistance Patterns Of HIV-1 Protease Mutants Selected under Drug Pressure

2. Macromolecular binding

3. Study of strong to ultratight protein interactions using differential scanning calorimetry

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