Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics
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Diverse sequences are functional at the C-terminus of the E. coli periplasmic chaperone SurA.
SurA is a major periplasmic molecular chaperone in Escherichia coli and has been shown to assist the biogenesis of several outer membrane proteins. The C-terminal fragment of SurA folds into a short β-strand, which forms a small three-stranded anti-parallel β-sheet module with the N-terminal β-hairpin. We found that the length of the C-terminal fragment, rather than its exact amino acid composi...
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ژورنال
عنوان ژورنال: PROTEOMICS
سال: 2009
ISSN: 1615-9853
DOI: 10.1002/pmic.200800794