Generation of a highly active folding enzyme by combining a parvulin-type prolyl isomerase from sura with an unrelated chaperone domain

Journal of Molecular Biology

Volumn 425, Issue 22, 2013, Pages 4089-4098

  Geitner, Anne Juliane ^a   Varga, Edina ^a   Wehmer, Marc ^a   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

artificial enzyme; domain insertion; folding catalysis; protein folding; SlyD

Indexed keywords

CHAPERONE; CHIMERIC PROTEIN; METHIONINE; PEPTIDYLPROLYL ISOMERASE; PROLYL ISOMERASE PAR1; PROLYL ISOMERASE PAR2; PROTEIN SLYD; SURVIVAL PROTEIN A; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME KINETICS; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STOICHIOMETRY;

ESCHERICHIA COLI;

EID: 84886726061     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.06.038     Document Type: Article

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