Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer

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

Volumn 108, Issue 41, 2011, Pages 16932-16937

  Guinn, Emily J ^a   Pegram, Laurel M ^a   Capp, Michael W ^a   Pollock, Michelle N ^a   Record Jr , M Thomas ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALIPHATIC HYDROCARBON; AMIDE; AROMATIC HYDROCARBON; BETAINE; HYDROGEN; UREA;

ARTICLE; CHEMICAL ANALYSIS; HUMAN; HYDRATION; HYDROGEN BOND; MOLECULAR DYNAMICS; PARTITION COEFFICIENT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PROCESSING; PROTEIN STABILITY; QUANTITATIVE ANALYSIS; SOLUBILITY;

BETAINE; BINDING SITES; HYDROGEN BONDING; MODELS, CHEMICAL; MOLECULAR DYNAMICS SIMULATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEINS; UREA;

EID: 80054717093     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1109372108     Document Type: Article

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