Protein cold denaturation as seen from the solvent

Journal of the American Chemical Society

Volumn 131, Issue 3, 2009, Pages 1025-1036

  Davidovic, Monika ^a   Mattea, Carlos ^a,b   Qvist, Johan ^a   Halle, Bertil ^a  

^a LUND UNIVERSITY   (Sweden)

^b ILMENAU UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

APOMYOGLOBIN; AQUEOUS SOLUBILITY; AQUEOUS SOLUTIONS; COLD DENATURATION; DENATURED STATE; EMULSION DROPLETS; GLOBULAR PROTEINS; HYDRATION DYNAMICS; HYDROPHOBIC DRIVING FORCES; ICE FORMATIONS; LACTOGLOBULIN; LOW TEMPERATURES; LOW WATER-CONTENT; MOLECULAR SYSTEMS; NATIVE STATE; NONPOLAR MOLECULES; PROTEIN SOLUTION; REVERSE MICELLES; ROOM TEMPERATURE; SPIN RELAXATION; TEMPERATURE DEPENDENT; TEMPERATURE RANGE; THERMODYNAMICALLY STABLE; UBIQUITIN; WATER INTERACTIONS;

COOLING SYSTEMS; EMULSIFICATION; EMULSIONS; HYDRATION; METABOLISM; PROTEIN FOLDING; SOLVENTS; SPIN DYNAMICS; UREA; WATER CONTENT;

DENATURATION;

APOMYOGLOBIN; BETA LACTOGLOBULIN; BOVINE PANCREATIC TRYPSIN INHIBIITOR; SOLVENT; TRYPSIN INHIBITOR; UBIQUITIN; UNCLASSIFIED DRUG; PROTEIN; WATER;

ARTICLE; HYDRATION; HYDROPHOBICITY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE; THERMOSTABILITY; CHEMISTRY; COLD; PH;

COLD TEMPERATURE; HYDROGEN-ION CONCENTRATION; PROTEIN DENATURATION; PROTEINS; SOLVENTS; WATER;

EID: 61749085446     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja8056419     Document Type: Article

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