Refolding and structural characterization of the human p53 tumor suppressor protein

Biophysical Chemistry

Volumn 96, Issue 2-3, 2002, Pages 243-257

  Bell, Stefan ^a   Hansen, Silke ^b   Buchner, Johannes ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b ROCHE DIAGNOSTICS GMBH   (Germany)

Author keywords

Cancer; Loosely folded protein; p53; Protein folding; Renaturation

Indexed keywords

ANTIBODY; PROTEIN P53; DNA BINDING PROTEIN; RECOMBINANT PROTEIN; TUMOR SUPPRESSOR PROTEIN;

ALLOSTERISM; ARTICLE; CANCER INHIBITION; CARBOXY TERMINAL SEQUENCE; CELL INCLUSION; CIRCULAR DICHROISM; CONFORMATION; CONTROLLED STUDY; CROSS LINKING; CYTOSOL; DNA BINDING; ESCHERICHIA COLI; FLUORESCENCE; GEL FILTRATION; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; RENATURATION; SPECTROSCOPY; CHEMISTRY; GEL MOBILITY SHIFT ASSAY; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; PROTEIN RENATURATION; STRUCTURE ACTIVITY RELATION;

ESCHERICHIA COLI;

CIRCULAR DICHROISM; DNA-BINDING PROTEINS; ELECTROPHORETIC MOBILITY SHIFT ASSAY; ESCHERICHIA COLI; HUMANS; INCLUSION BODIES; PROTEIN RENATURATION; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR SUPPRESSOR PROTEIN P53; TUMOR SUPPRESSOR PROTEINS;

EID: 0037007442     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00011-X     Document Type: Article

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