Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases

Protein Science

Volumn 13, Issue 9, 2004, Pages 2378-2387

  Kühlewein, Angelika ^a   Voll, Georg ^a   Alvarez, Birte Hernandez ^b   Kessler, Horst ^a   Fischer, Gunter ^b   Rahfeld, Jens Ulrich ^b   Gemmecker, Gerd ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b M P Forschungsstelle Enzymol P   (Germany)

Author keywords

Cis peptide bond; NMR; Parvulin; PPIase; Protein structure

Indexed keywords

CYCLOPHILIN; OLIGOPEPTIDE; PARVULIN; PROTEIN; PROTEIN HPAR14; PROTEIN HPIN1; PROTEIN PAR10; PROTEIN PIN1AT; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CHEMICAL BOND; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SPECIFICITY; ESCHERICHIA COLI; HYDROGEN BOND; HYDROPHOBICITY; ISOMERIZATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ESCHERICHIA COLI PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDYLPROLYL ISOMERASE; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS; STRUCTURAL HOMOLOGY, PROTEIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 4344679004     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04756704     Document Type: Article

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