The periplasmic E. coli chaperone Skp is a trimer in solution: Biophysical and preliminary crystallographic characterization

Biological Chemistry

Volumn 385, Issue 2, 2004, Pages 137-143

  Schlapschy, Martin ^a   Dommel, Monica K ^a   Hadian, Kamyar ^a   Fogarasi, Marton ^a   Korndörfer, Ingo P ^a   Skerra, Arne ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Circular dichroism; Cross linking; Outer membrane protein; Protein folding; Strep tag; Thermal denaturation

Indexed keywords

CHAPERONE; ESCHERICHIA COLI PROTEIN; PERIPLASMIC PROTEIN; RECOMBINANT PROTEIN; S PHASE KINASE ASSOCIATED PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BIOPHYSICS; CIRCULAR DICHROISM; CRYSTALLIZATION; CYTOPLASM; ESCHERICHIA COLI; GEL FILTRATION CHROMATOGRAPHY; HYSTERESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CROSS LINKING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; THERMAL STIMULATION; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PERIPLASM; PERIPLASMIC PROTEINS; PROTEIN DENATURATION; PROTEIN RENATURATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

HOMO; NEGIBACTERIA;

EID: 1842787813     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2004.032     Document Type: Article

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