Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to αB-crystallin

Journal of Biological Chemistry

Volumn 278, Issue 45, 2003, Pages 44214-44221

  Sathish, Hasige A ^b   Stein, Richard A ^b   Yang, Guangyong ^b   McHaourab, Hassane S ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; CONFORMATIONS; FLUORESCENCE; ISOTHERMS; QUENCHING;

CHAPERONE;

ENZYMES;

ALPHA CRYSTALLIN; BROMOBIMANE; CHAPERONE; FLUORESCENT DYE; HEAT SHOCK PROTEIN; LYSOZYME; MUTANT PROTEIN; SOLVENT;

ANALYTIC METHOD; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; CORRELATION ANALYSIS; ENERGY; ENZYME SUBSTRATE; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; ISOTHERM; LENS; MODEL; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; REGULATORY MECHANISM; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS;

ALPHA-CRYSTALLIN B CHAIN; BACTERIOPHAGE T4; BICYCLO COMPOUNDS, HETEROCYCLIC; BINDING SITES; FLUORESCENCE; HEAT-SHOCK PROTEINS; HYDROGEN-ION CONCENTRATION; INDICATORS AND REAGENTS; MOLECULAR CHAPERONES; MURAMIDASE; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE; THERMODYNAMICS;

EID: 0242582458     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M307578200     Document Type: Article

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