The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins

Proceedings of the National Academy of Sciences of the United States of America

Volumn 95, Issue 4, 1998, Pages 1552-1555

  Hummer, Gerhard ^a   Garde, Shekhar ^a,b   García, Angel E ^a   Paulaitis, Michael E ^c   Pratt, Lawrence R ^a  

^a LOS ALAMOS NATIONAL LABORATORY   (United States)

^b University of Delaware   (United States)

^c Johns Hopkins University   (United States)

Author keywords

Activation volumes; Hydrophobic effect; Protein folding; Protein folding kinetics; Protein unfolding

Indexed keywords

AQUEOUS SOLUTION; ARTICLE; ENERGY TRANSFER; ENTROPY; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

HYDROSTATIC PRESSURE; KINETICS; METHANE; MODELS, CHEMICAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; SOLUBILITY; SOLVENTS; THERMODYNAMICS; WATER;

EID: 0032539604     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.95.4.1552     Document Type: Article

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