Equilibrium folding of pro-HlyA from Escherichia coli reveals a stable calcium ion dependent folding intermediate

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1844, Issue 9, 2014, Pages 1500-1510

  Thomas, Sabrina ^a   Bakkes, Patrick J ^a   Smits, Sander H J ^a   Schmitt, Lutz ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

Author keywords

Calcium; Folding mechanics; HlyA; Protein folding; RTX; Tryptophan fluorescence

Indexed keywords

BACTERIAL PROTEIN; CALCIUM ION; HLYA PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; ESCHERICHIA COLI; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN SECRETION; PROTEIN STABILITY; PROTEIN UNFOLDING;

CALCIUM; FOLDING MECHANICS; HLYA; PROTEIN FOLDING; RTX; TRYPTOPHAN FLUORESCENCE;

BACTERIAL SECRETION SYSTEMS; CALCIUM; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION; HEMOLYSIN PROTEINS; KINETICS; MUTATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PRECURSORS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TRYPTOPHAN; UREA;

EID: 84902295043     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.05.006     Document Type: Article

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