The small heat-shock chaperone protein, α-crystallin, does not recognise stable molten globule states of cytosolic proteins

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1481, Issue 1, 2000, Pages 175-188

  Treweek, Teresa M ^a   Lindner, Robyn A ^a   Mariani, Michael ^a   Carver, John A ^a  

^a UNIVERSITY OF WOLLONGONG   (Australia)

Author keywords

Chaperone protein; Glycation; Molten globule state; Spectroscopy

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; CYTOSOL RECEPTOR; GLUCOSE 6 PHOSPHATE; HEAT SHOCK PROTEIN;

ANIMAL CELL; ARTICLE; CATTLE; CHEMICAL REACTION KINETICS; COMPLEX FORMATION; LENS; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; NONHUMAN; PRECIPITATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION;

ANILINO NAPHTHALENESULFONATES; ANIMALS; BINDING SITES; CATTLE; CIRCULAR DICHROISM; CRYSTALLINS; CYTOSOL; FLUORESCENT DYES; GLUCOSE-6-PHOSPHATE; GLYCOPROTEINS; GLYCOSYLATION; HEAT-SHOCK PROTEINS; LENS, CRYSTALLINE; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR CHAPERONES; MOLECULAR WEIGHT; MYOGLOBIN; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; SPECTROMETRY, MASS, SECONDARY ION; TEMPERATURE;

ANIMALIA; BOS TAURUS;

EID: 0034739275     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00109-6     Document Type: Article

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