Origins of protein denatured state compactness and hydrophobic clustering in aqueous urea: Inferences from nonpolar potentials of mean force

Proteins: Structure, Function and Genetics

Volumn 49, Issue 4, 2002, Pages 560-566

  Shimizu, Seishi ^a   Chan, Hue Sun ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

Compact denatured states; Heat capacity; Hydrophobicity; m value; Solvent accessible surface area; Urea denaturation

Indexed keywords

PROTEIN; UREA; WATER;

AQUEOUS SOLUTION; ARTICLE; CALCULATION; ENERGY; ENERGY TRANSFER; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN FOLDING;

CALORIMETRY; COMPUTER SIMULATION; HYDROPHOBICITY; METHANE; MODELS, MOLECULAR; PENTANES; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; SOLUBILITY; SOLUTIONS; SOLVENTS; TEMPERATURE; THERMODYNAMICS; UREA;

EID: 0036891682     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10263     Document Type: Article

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