Chaperone SecB: Conformational changes demonstrated by circular dichroism
- 1 October 1995
- journal article
- research article
- Published by Springer Nature in Protein Journal
- Vol. 14 (7) , 595-600
- https://doi.org/10.1007/bf01886885
Abstract
The chaperone SecB, which is involved in protein export inEscherichia coli, is shown by circular dichroism measurements to contain a high content ofβ-pleated sheets. Prediction of the secondary structure of SecB is in good agreement with the observed content ofβ-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.Keywords
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