Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity

Journal of Biological Chemistry

Volumn 287, Issue 8, 2012, Pages 5661-5672

  Xu, Xinping ^a   Sarbeng, Evans Boateng ^a   Vorvis, Christina ^a   Kumar, Divya Prasanna ^a   Zhou, Lei ^a   Liu, Qinglian ^a  

^a VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC RESIDUES; CHAPERONE ACTIVITY; FAST KINETICS; HEAT-SHOCK PROTEIN; MECHANISTIC DIFFERENCES; MOLECULAR CHAPERONES; PEPTIDE SUBSTRATES; PEPTIDE-BINDING; PROTEIN AGGREGATION; SUBSTRATE BINDING;

PEPTIDES; SUBSTRATES;

BINDING ENERGY;

CHAPERONE; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 70;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; BINDING SITES; HSP110 HEAT-SHOCK PROTEINS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS; PEPTIDES; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 84863155446     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.275057     Document Type: Article

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