The Folding Process of Acylphosphatase from Escherichia coli is Remarkably Accelerated by the Presence of a Disulfide Bond

Journal of Molecular Biology

Volumn 379, Issue 5, 2008, Pages 1107-1118

  Parrini, Claudia ^a   Bemporad, Francesco ^a   Baroncelli, Alessio ^a   Gianni, Stefano ^b   Travaglini Allocatelli, Carlo ^b   Kohn, Jonathan E ^c   Ramazzotti, Matteo ^a   Chiti, Fabrizio ^a   Taddei, Niccolò ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

^c University of California at Berkeley   (United States)

Author keywords

intermediate; protein folding; reduced; thiol; three state folding

Indexed keywords

ACYLPHOSPHATASE; ALANINE; CYSTEINE;

ARTICLE; CIRCULAR DICHROISM; DISULFIDE BOND; ESCHERICHIA COLI; HYDROPHOBICITY; LIGHT SCATTERING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING;

ESCHERICHIA COLI;

EID: 44349147790     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.04.051     Document Type: Article

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