Binding of destabilized βB2-crystallin mutants to α-crystallin: The role of a folding intermediate

Journal of Biological Chemistry

Volumn 279, Issue 16, 2004, Pages 16425-16432

  Sathish, Hasige A ^a   Koteiche, Hanane A ^a   Mchaourab, Hassane S ^a  

^a VANDERBILT UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; CELLS; FLUORESCENCE; MONOMERS; MUTAGENESIS; PROTEINS;

FIBER CELLS; FLUORESCENT PROBES;

BIOCHEMISTRY;

ALPHA CRYSTALLIN; BETA B2 CRYSTALLIN; BETA CRYSTALLIN; CHAPERONE; DIMER; FLUORESCENT DYE; LYSOZYME; MONOMER; MUTANT PROTEIN; SOLVENT; UNCLASSIFIED DRUG; BETA CRYSTALLIN B2; BETA-CRYSTALLIN B2; DRUG DERIVATIVE;

ARTICLE; BINDING AFFINITY; ENERGY; MOLECULAR MODEL; MOLECULAR PROBE; MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; AGING; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; MOUSE; PHYSIOLOGY; STRUCTURE ACTIVITY RELATION;

AGING; ALPHA-CRYSTALLINS; ANIMALS; BETA-CRYSTALLIN B CHAIN; BINDING SITES; MICE; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 1942437441     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M313402200     Document Type: Article

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