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Volumn 40, Issue 34, 2001, Pages 10317-10325

Insights into the stability of native and partially folded states of ubiquitin: Effects of cosolvents and denaturants on the thermodynamics of protein folding

(2) Jourdan, M a Searle, M S a

a UNIVERSITY OF NOTTINGHAM (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DENATURANTS; PROTEIN FOLDINGS;

CHLORINE COMPOUNDS; ENTHALPY; ENTROPY; HYDROPHOBICITY; METHANOL; ORGANIC SOLVENTS; THERMODYNAMICS;

PROTEINS;

GUANIDINE; HYDROCARBON; METHANOL; SOLVENT; UBIQUITIN;

ARTICLE; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; ENTHALPY; ENTROPY; EXPERIMENTAL MODEL; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN STABILITY; SOLUBILITY;

ANIMALS; CALORIMETRY; CATTLE; CIRCULAR DICHROISM; GUANIDINE; METHANOL; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; THERMODYNAMICS; UBIQUITINS;

EID: 0035964184 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi010767j Document Type: Article

Times cited : (39)

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