Chaperone SecB: conformational changes demonstrated by circular dichroism
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 th...
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Published in | Journal of protein chemistry Vol. 14; no. 7; p. 595 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
01.10.1995
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Subjects | |
Online Access | Get more information |
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Summary: | 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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ISSN: | 0277-8033 |
DOI: | 10.1007/BF01886885 |