The carboxy-terminal domain of heat-shock factor 1 is largely unfolded but can be induced to collapse into a compact, partially structured state

Biochemistry

Volumn 46, Issue 11, 2007, Pages 3405-3415

  Pattaramanon, Narinporn ^b   Sangha, Navneet ^a   Gafni, Ari ^a,b,c  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^c UNIVERSITY OF MICHIGAN HEALTH SYSTEM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; BINDING ENERGY; CATIONIC SURFACTANTS; DICHROISM; HYDROPHOBICITY; PROTEOLYSIS; SIZE EXCLUSION CHROMATOGRAPHY; THERMAL EFFECTS;

HEAT-SHOCK TRANSCRIPTION FACTORS; PHYSIOLOGICAL CONDITIONS; PROTEOLYTIC CLEAVAGE;

PROTEINS;

CATIONIC SURFACTANT; HEAT SHOCK PROTEIN; HEAT SHOCK TRANSCRIPTION FACTOR 1; NAPHTHALENESULFONIC ACID DERIVATIVE; TRIFLUOROETHANOL; TRIMETHYLAMINE OXIDE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; GEL PERMEATION CHROMATOGRAPHY; HEAT SHOCK RESPONSE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDRODYNAMICS; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; REGULATORY MECHANISM; TRANSCRIPTION INITIATION;

CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; COMPUTATIONAL BIOLOGY; DNA-BINDING PROTEINS; HEAT-SHOCK PROTEINS; HYDROPHOBICITY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; TRANSCRIPTION FACTORS;

EID: 33947408308     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061124c     Document Type: Article

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