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Chaperone SecB: conformational changes demonstrated by circular dichroism.

G D Fasman·K Park·L L Randall
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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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Bacterial ProteinsCircular DichroismMolecular ChaperonesProtein ConformationProtein Structure, SecondarySodium ChlorideJournal ArticleResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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G D Fasman, K Park, L L Randall. 1995. Chaperone SecB: conformational changes demonstrated by circular dichroism.. https://doi.org/10.1007/bf01886885

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