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Volumn 277, Issue 1, 2002, Pages 735-745
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Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain
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Author keywords
[No Author keywords available]
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Indexed keywords
CARBOXYLATION;
HYDROPHOBICITY;
OLIGOMERS;
PROTEINS;
RELAXATION PROCESSES;
YEAST;
HEAT SHOCK FACTOR-BINDING PROTEIN (HSBP);
BIOCHEMISTRY;
HEAT SHOCK FACTOR BINDING PROTEIN 1;
HEAT SHOCK PROTEIN;
PROTEINASE;
UNCLASSIFIED DRUG;
ALPHA HELIX;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
GENETIC CONSERVATION;
HYDROPHOBICITY;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
NUCLEOTIDE SEQUENCE;
OLIGOMERIZATION;
POLYACRYLAMIDE GEL ELECTROPHORESIS;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN DOMAIN;
PROTEIN FAMILY;
PROTEIN FOLDING;
PROTEIN INTERACTION;
PROTEIN MOTIF;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
ULTRACENTRIFUGATION;
AMINO ACID SEQUENCE;
CHROMATOGRAPHY, GEL;
CONSERVED SEQUENCE;
HEAT-SHOCK PROTEINS;
HUMANS;
HYDROPHOBICITY;
MOLECULAR SEQUENCE DATA;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
REPETITIVE SEQUENCES, AMINO ACID;
STRUCTURE-ACTIVITY RELATIONSHIP;
ULTRACENTRIFUGATION;
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EID: 0037016744
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M108604200 Document Type: Article |
Times cited : (38)
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References (71)
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