Deletion of 54FLRAPSWF61 residues decreases the oligomeric size and enhances the chaperone function of αB-crystallin

Biochemistry

Volumn 48, Issue 23, 2009, Pages 5066-5073

  Santhoshkumar, Puttur ^a   Murugesan, Raju ^a   Sharma, K Krishna ^a  

^a University of Missouri   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE ACTION; CHAPERONE ACTIVITY; CHAPERONE FUNCTIONS; CRYSTALLIN; DELETION MUTANTS; DISULFONIC ACID; HIGHER ORDER; HOMO-OLIGOMERS; INTRINSIC TRYPTOPHAN FLUORESCENCES; MULTI-ANGLE LIGHT SCATTERINGS; MUTANT PROTEINS; N-TERMINAL DOMAINS; SMALL HEAT SHOCK PROTEINS; SUBUNIT EXCHANGE; TARGET PROTEINS; WILD TYPES; WILD-TYPE PROTEINS;

AMINES; AMINO ACIDS; BIOCHEMISTRY; NAPHTHALENE; OLIGOMERS;

HYDROPHOBICITY;

1,10 BI(4 ANILINO)NAPHTHALENE 5,50 DISULFONIC ACID; ALPHA CRYSTALLIN; CHAPERONE; MUTANT PROTEIN; OLIGOMER; PHENYLALANINE DERIVATIVE; PHENYLALANYLLEUCYLARGINYLALANYLSERYLTRYPTOPHYLPHENYLALANINE; PROTEIN SUBUNIT; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; DELETION MUTANT; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; LIGHT SCATTERING; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; WILD TYPE;

ALPHA-CRYSTALLIN A CHAIN; ALPHA-CRYSTALLIN B CHAIN; AMINO ACID SEQUENCE; BINDING SITES; CIRCULAR DICHROISM; HUMANS; MICROSCOPY, ELECTRON, TRANSMISSION; MOLECULAR SEQUENCE DATA; PROTEIN SUBUNITS; SEQUENCE DELETION;

EID: 67049100601     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900085v     Document Type: Article

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