Home
About
Overview
Sharing Data
ORCID
Help
History (94)
HIV-1 protease inhibitors from inverse design in the substrate envelope exhibit subnanomolar binding to drug-resistant variants.
TMC310911, a novel human immunodeficiency virus type 1 protease inhibitor, shows in vitro an improved resistance profile and higher genetic barrier to resistance compared with current protease inhibitors.
Exploring the role of the solvent in the denaturation of a protein: a molecular dynamics study of the DNA binding domain of the 434 repressor.
Promise of advances in simulation methods for protein crystallography: implicit solvent models, time-averaging refinement, and quantum mechanical modeling.
Hydrophobic core flexibility modulates enzyme activity in HIV-1 protease.
See All 94 Pages
Login
to edit your profile (add a photo, awards, links to other websites, etc.)
Edit My Profile
My Person List (
0
)
Return to Top
Hydrophobic core flexibility modulates enzyme activity in HIV-1 protease.
Mittal S, Cai Y, Nalam MN, Bolon DN, Schiffer CA. Hydrophobic core flexibility modulates enzyme activity in HIV-1 protease. J Am Chem Soc. 2012 Mar 07; 134(9):4163-8.
View in:
PubMed
subject areas
Crystallography, X-Ray
Enzyme Activation
HIV Protease
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Molecular Dynamics Simulation
Mutation
Protein Conformation
authors with profiles
Celia A Schiffer PhD
Daniel N Bolon PhD