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Updated: Aug 7, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Chaperone SecB: conformational changes demonstrated by circular dichroism
G D Fasman1, K Park, L L Randall
1Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254, USA.
Abstract:
The chaperone SecB, which is involved in protein export in Escherichia coli, is shown by circular dichroism measurements to contain a high content of beta-pleated sheets. Prediction of the secondary structure of SecB is in good agreement with the observed content of beta-sheet. In accordance with the previous studies in which changes in conformation were assessed indirectly [Randall (1992), Science 257, 241-245], here we show that the conformation of SecB changes with the concentration of salt in the milieu and also when SecB interacts with a peptide ligand.
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