PPIase domain of trigger factor acts as auxiliary chaperone site to assist the folding of protein substrates bound to the crevice of trigger factor

International Journal of Biochemistry and Cell Biology

Volumn 42, Issue 6, 2010, Pages 890-901

  Liu, Chuan Peng ^a,b   Zhou, Qi Ming ^b   Fan, Dong Jie ^b   Zhou, Jun Mei ^b  

^a HARBIN INSTITUTE OF TECHNOLOGY   (China)

^b INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Chaperone; Modulation of chaperone function; Peptidyl prolyl cis trans isomerase domain; Protein folding; Trigger factor

Indexed keywords

CARBONATE DEHYDRATASE II; CHAPERONE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LYSOZYME; MUTANT PROTEIN; PEPTIDYLPROLYL ISOMERASE; TRIGGER FACTOR; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; GENE DELETION; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMALS; CARBONIC ANHYDRASE II; CATALYTIC DOMAIN; CATTLE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE (PHOSPHORYLATING); HUMANS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PEPTIDYLPROLYL ISOMERASE; PROTEIN ENGINEERING; PROTEIN FOLDING; RABBITS; STRUCTURE-ACTIVITY RELATIONSHIP; SWINE;

EID: 77953811357     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2010.01.019     Document Type: Article

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