Combination of the human prolyl isomerase FKBP12 with unrelated chaperone domains leads to chimeric folding enzymes with high activity

Journal of Molecular Biology

Volumn 420, Issue 4-5, 2012, Pages 335-349

  Geitner, Anne Juliane ^a   Schmid, Franz Xaver ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

artificial enzymes; domain insertion; GroEL; protein disulfide isomerase; SurA

Indexed keywords

CHAPERONE; PEPTIDYLPROLYL ISOMERASE; PROTEIN DISULFIDE ISOMERASE; PROTEIN FKBP12; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CYTOPLASM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING;

ESCHERICHIA COLI;

EID: 84862224971     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.04.018     Document Type: Article

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