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Volumn 410, Issue 1, 2008, Pages 63-70
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The dramatically increased chaperone activity of small heat-shock protein IbpB is retained for an extended period of time after the stress condition is removed
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Author keywords
Chaperone activity; Inclusion body binding protein B (IbpB); Molecular chaperone; Small heat shock protein (sHSP); Structural flexibility
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Indexed keywords
CHAPERONE ACTIVITY;
MOLECULAR CHAPERONE;
STRUCTURAL FLEXIBILITY;
BINDING SITES;
COMPLEXATION;
ENZYME ACTIVITY;
ESCHERICHIA COLI;
HYDROPHOBICITY;
PROTEINS;
CHAPERONE;
INCLUSION BODY BINDING PROTEIN B;
PROTEIN SUBUNIT;
SMALL HEAT SHOCK PROTEIN;
UNCLASSIFIED DRUG;
ARTICLE;
HEAT SHOCK;
HYDROPHOBICITY;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN DEGRADATION;
PROTEIN FUNCTION;
STRESS;
CHROMATOGRAPHY, GEL;
CIRCULAR DICHROISM;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
FLUORESCENCE RESONANCE ENERGY TRANSFER;
HEAT-SHOCK PROTEINS;
HEAT-SHOCK RESPONSE;
HYDROLYSIS;
MOLECULAR CHAPERONES;
SPECTROMETRY, FLUORESCENCE;
ESCHERICHIA COLI;
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EID: 39749148886
PISSN: 02646021
EISSN: None
Source Type: Journal
DOI: 10.1042/BJ20071120 Document Type: Article |
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Times cited : (21)
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References (52)
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