Hyperquenching and cold equilibration strategies for the study of liquid-liquid and protein folding transitions

Biophysical Chemistry

Volumn 105, Issue 2-3, 2003, Pages 621-637

  Angell, C Austen ^a   Wang, Li Min ^a  

^a ARIZONA STATE UNIVERSITY   (United States)

Author keywords

Aggregation; Cold refolding; Crystallization; Energy landscape; Fictive temperature; Glass transition; Hyperquench; Liquid liquid transition; Protein folding; Renaturation

Indexed keywords

AMMONIUM DERIVATIVE; GLASS; ICE; LYSOZYME; NITRIC ACID DERIVATIVE; PROTEIN; SOLVENT; SUCROSE;

AQUEOUS SOLUTION; ARTICLE; CALORIMETRY; CHEMICAL PROCEDURES; CHEMICAL STRUCTURE; COLD; COOLING; CRYSTALLIZATION; ENTHALPY; ENTROPY; EVOLUTION; GLASS TRANSITION TEMPERATURE; HEATING; LIQUID; LOW TEMPERATURE PROCEDURES; MASS SPECTROMETRY; MOLECULAR MECHANICS; MOLECULE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN FOLDING; QUANTITATIVE ANALYSIS; STUDY; SYNTHESIS; TIME; VIBRATION;

EID: 0141453955     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(03)00093-0     Document Type: Article

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