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Volumn 41, Issue 26, 2002, Pages 8499-8507
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Characterization of two partially unfolded intermediates of the molecular chaperone DnaK at low pH
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Author keywords
[No Author keywords available]
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Indexed keywords
CHEMICAL ASSAYS;
CONFORMATIONS;
DYES;
ESCHERICHIA COLI;
HYDROPHOBICITY;
PH;
PROTEINS;
BIOCHEMISTRY;
8 ANILINO 1 NAPHTHALENESULFONIC ACID;
CATHEPSIN D;
CHAPERONE;
NUCLEOTIDE;
PROTEIN DNAK;
AMINO TERMINAL SEQUENCE;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
CONFORMATIONAL TRANSITION;
ESCHERICHIA COLI;
HYDROPHOBICITY;
NONHUMAN;
PH;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN DEGRADATION;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTEIN SECONDARY STRUCTURE;
ADENOSINE TRIPHOSPHATASES;
CALORIMETRY;
CIRCULAR DICHROISM;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
FLUORESCENT DYES;
HSP70 HEAT-SHOCK PROTEINS;
HYDROGEN-ION CONCENTRATION;
KINETICS;
MODELS, MOLECULAR;
MOLECULAR CHAPERONES;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
THERMODYNAMICS;
ESCHERICHIA COLI;
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EID: 0037007980
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi025810x Document Type: Article |
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Times cited : (12)
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References (39)
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