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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.
Hydrophobic core flexibility modulates enzyme activity in HIV-1 protease.
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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.
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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