The molecular chaperone α-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of α-lactalbumin

Biochemical Journal

Volumn 354, Issue 1, 2001, Pages 79-87

  Lindner, R A ^a   Treweek, T M ^a   Carver, J A ^a  

^a UNIVERSITY OF WOLLONGONG   (Australia)

Author keywords

Hofmeister salts; Small heat shock protein; Spectroscopy

Indexed keywords

ALPHA CRYSTALLIN; ALPHA LACTALBUMIN; CHAPERONE; HEAT SHOCK PROTEIN;

ARTICLE; ENZYME KINETICS; IN VIVO STUDY; MOLECULAR INTERACTION; MOLECULAR WEIGHT; NONHUMAN; PRECIPITATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE;

BINDING, COMPETITIVE; CRYSTALLINS; KINETICS; LACTALBUMIN; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR CHAPERONES; MOLECULAR WEIGHT; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPECTRUM ANALYSIS;

EID: 0035865589     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3540079     Document Type: Article

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