SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities

Biochemistry

Volumn 45, Issue 1, 2006, Pages 20-33

  Scholz, Christian ^a   Eckert, Barbara ^b   Hagn, Franz ^b,c   Schaarschmidt, Peter ^a   Balbach, Jochen ^b,d   Schmid, Franz Xaver ^b  

^a ROCHE DIAGNOSTICS GMBH   (Germany)

^b UNIVERSITY OF BAYREUTH   (Germany)

^c TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^d MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGY; ENERGY CONSERVATION; ESCHERICHIA COLI; MONOMERS;

CHAPERONE PROPERTIES; ECTODOMAIN FRAGMENT; PROLYL ISOMERASE; SLYD PROTEINS;

PROTEINS;

BACTERIAL PROTEIN; CHAPERONE; GLYCOPROTEIN GP 41; ISOMERASE; PROLINE; PROLYL ISOMERASE; PROTEIN SLYD; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BIOTECHNOLOGICAL PROCEDURES; CARBOXY TERMINAL SEQUENCE; CYTOSOL; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; ESCHERICHIA COLI; HUMAN IMMUNODEFICIENCY VIRUS 1; NONHUMAN; ORTHOLOGY; PASTEURELLA MULTOCIDA; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN ISOLATION; SOLUBILITY; SPECIES DIFFERENCE; TREPONEMA PALLIDUM; VIBRIO CHOLERAE; YERSINIA PESTIS;

AMINO ACID SEQUENCE; CATALYSIS; CYTOSOL; ESCHERICHIA COLI PROTEINS; HIV ENVELOPE PROTEIN GP41; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PEPTIDYLPROLYL ISOMERASE; PROLINE; RIBONUCLEASE T1; SOLUBILITY; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; HUMAN IMMUNODEFICIENCY VIRUS 1; PASTEURELLA MULTOCIDA; TREPONEMA PALLIDUM; VIBRIO CHOLERAE; YERSINIA PESTIS;

EID: 30144446085     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051922n     Document Type: Article

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