Structure, stability, and chaperone function of αA-crystallin: Role of N-terminal region

Biopolymers

Volumn 86, Issue 3, 2007, Pages 177-192

  Kundu, Madhuchhanda ^a   Sen, P C ^a   Das, K P ^a  

^a BOSE INSTITUTE   (India)

Author keywords

crystallin; Chaperone function; Deletion mutant; Molecular chaperone; N terminal region; Oligomeric size; Small heat shock proteins; Thermodynamic stability

Indexed keywords

ESCHERICHIA COLI; KETONES; OLIGOMERS; PROTEINS; SIZE EXCLUSION CHROMATOGRAPHY; THERMODYNAMIC STABILITY;

CHAPERONE FUNCTIONS; DELETION MUTANT; MOLECULAR CHAPERONE; OLIGOMERIC SIZE; SMALL HEAT SHOCK PROTEINS;

CRYSTAL STRUCTURE;

ALPHA CRYSTALLIN; CHAPERONE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; GEL PERMEATION CHROMATOGRAPHY; HYDROPHOBICITY; MOLECULAR WEIGHT; OLIGOMERIZATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

ALPHA-CRYSTALLIN A CHAIN; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BUFFERS; CATTLE; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CLONING, MOLECULAR; DIMERIZATION; ESCHERICHIA COLI; GENE DELETION; HEAT-SHOCK PROTEINS, SMALL; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; KINETICS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PHOSPHATES; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN RENATURATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TEMPERATURE; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 34250323941     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.20716     Document Type: Article

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