Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD

Biological Chemistry

Volumn 394, Issue 8, 2013, Pages 965-975

  Kovermann, Michael ^a   Schmid, Franz X ^b   Balbach, Jochen ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

Chaperone; Enzyme mechanism; Nickel metalloprotein; Prolyl isomerase; Protein folding

Indexed keywords

ARGININE; BACTERIAL PROTEIN; FK 506 BINDING PROTEIN; HELPER FACTOR; HISTIDINE; HYDROGENASE; METALLOCHAPERONE; METALLOCHAPERONE SLYD; NICKEL; NICKEL IRON HYDROGENASE; PEPTIDYLPROLYL ISOMERASE; PROLINE; PROTEIN VARIANT; RAPAMYCIN; RIBONUCLEASE T1; SIGNAL PEPTIDE; TACROLIMUS; TETRAPEPTIDE; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

BACTERIAL TRANSLOCATION; BACTERIOPHAGE; BACTERIOPHAGE PHI X 174; BINDING SITE; BIOPHYSICS; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CATALYST; CHEMICAL ANALYSIS; CHIMERA; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; METAL BINDING; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN REFOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; PROTON NUCLEAR MAGNETIC RESONANCE; REVIEW; SEQUENCE ALIGNMENT; THERMUS THERMOPHILUS; X RAY CRYSTALLOGRAPHY; BACTERIA; CHEMISTRY; CONFORMATION; METABOLISM;

BACTERIA (MICROORGANISMS);

BACTERIA; BACTERIAL PROTEINS; METALLOCHAPERONES; MOLECULAR CONFORMATION; PEPTIDYLPROLYL ISOMERASE; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 84881659500     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2013-0137     Document Type: Review

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