Structure and mechanism of protein stability sensors: Chaperone activity of small heat shock proteins

Biochemistry

Volumn 48, Issue 18, 2009, Pages 3828-3837

  Mchaourab, Hassane S ^a,b   Godar, Jared A ^a   Stewart, Phoebe L ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b VANDERBILT UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR CONDITIONS; CHAPERONE ACTIVITY; CHEMICAL ENERGY; CONCEPTUAL FRAMEWORKS; CONTROLLED SWITCHING; DISEASE STATE; MISFOLDING; MOLECULAR CHAPERONES; PATHOLOGICAL PROCESS; PROTEIN STABILITY; SMALL HEAT SHOCK PROTEINS; STRUCTURAL BASIS; THERMODYNAMIC EQUILIBRIA;

CHEMICAL MODIFICATION; CHEMICAL STABILITY; SENSORS;

PROTEINS;

ALPHA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN; OLIGOMER;

BINDING AFFINITY; CHEMICAL MODIFICATION; MOLECULAR RECOGNITION; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; THERMODYNAMICS;

DIMERIZATION; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEAT-SHOCK PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PROTEIN CONFORMATION; THERMODYNAMICS;

EID: 66149117827     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900212j     Document Type: Review

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