Mechanism of chaperone function in small heat shock proteins: Two-mode binding of the excited states of T4 lysozyme mutants by αA-crystallin

Journal of Biological Chemistry

Volumn 277, Issue 43, 2002, Pages 40557-40566

  Mchaourab, Hassane S ^a,b   Dodson, Erich K ^a   Koteiche, Hanane A ^b  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b VANDERBILT UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; CRYSTAL STRUCTURE; FREE ENERGY; PARAMAGNETIC RESONANCE; PH EFFECTS; PROTEINS; STOICHIOMETRY; THERMODYNAMICS;

CRYSTALLIN CHAPERONE FUNCTIONS;

BIOCHEMISTRY;

ALPHA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN; LYSOZYME;

ARTICLE; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; SITE DIRECTED MUTAGENESIS; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

BACTERIOPHAGE T4; CRYSTALLINS; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEAT-SHOCK PROTEINS; HYDROGEN-ION CONCENTRATION; MOLECULAR CHAPERONES; MURAMIDASE; MUTATION; PROTEIN BINDING; TEMPERATURE;

EID: 0037174851     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M206250200     Document Type: Article

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