u-75875 and 85548e

u-75875 has been researched along with 85548e* in 1 studies

Other Studies

1 other study(ies) available for u-75875 and 85548e

Article	Year
A mean field model of ligand-protein interactions: implications for the structural assessment of human immunodeficiency virus type 1 protease complexes and receptor-specific binding. Proceedings of the National Academy of Sciences of the United States of America, 1996, Jan-09, Volume: 93, Issue:1 We propose a general mean field model of ligand-protein interactions to determine the thermodynamic equilibrium of a system at finite temperature. The method is employed in structural assessments of two human immuno-deficiency virus type 1 protease complexes where the gross effects of protein flexibility are incorporated by utilizing a data base of crystal structures. Analysis of the energy spectra for these complexes has revealed that structural and thermo-dynamic aspects of molecular recognition can be rationalized on the basis of the extent of frustration in the binding energy landscape. In particular, the relationship between receptor-specific binding of these ligands to human immunodeficiency virus type 1 protease and a minimal frustration principle is analyzed. Topics: Aspartic Acid Endopeptidases; HIV Protease; HIV Protease Inhibitors; HIV-1; Ligands; Oligopeptides; Protein Binding; Protein Conformation; Temperature; Thermodynamics	1996

Article

Year

A mean field model of ligand-protein interactions: implications for the structural assessment of human immunodeficiency virus type 1 protease complexes and receptor-specific binding.

Proceedings of the National Academy of Sciences of the United States of America, 1996, Jan-09, Volume: 93, Issue:1

We propose a general mean field model of ligand-protein interactions to determine the thermodynamic equilibrium of a system at finite temperature. The method is employed in structural assessments of two human immuno-deficiency virus type 1 protease complexes where the gross effects of protein flexibility are incorporated by utilizing a data base of crystal structures. Analysis of the energy spectra for these complexes has revealed that structural and thermo-dynamic aspects of molecular recognition can be rationalized on the basis of the extent of frustration in the binding energy landscape. In particular, the relationship between receptor-specific binding of these ligands to human immunodeficiency virus type 1 protease and a minimal frustration principle is analyzed.

Topics: Aspartic Acid Endopeptidases; HIV Protease; HIV Protease Inhibitors; HIV-1; Ligands; Oligopeptides; Protein Binding; Protein Conformation; Temperature; Thermodynamics

1996