Chaperone SecB: Conformational changes demonstrated by circular dichroism |
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| Authors: | Gerald D. Fasman Kyusung Park Linda L. Randall |
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| Affiliation: | (1) Graduate Department of Biochemistry, Brandeis University, 02254 Waltham, Massachusetts;(2) Present address: Lineberger Cancer Research Center, University of North Carolina School of Medicine, 02715 Chapel Hill, North Carolina;(3) Department of Biochemistry and Biophysics, Washington State University, 99164-4660 Pullman, Washington |
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| Abstract: | The chaperone SecB, which is involved in protein export inEscherichia coli, is shown by circular dichroism measurements to contain a high content of -pleated sheets. Prediction of the secondary structure of SecB is in good agreement with the observed content of-sheet. In accordance with the previous studies in which changes in conformation were assessed indirectly [Randall (1992),Science257, 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.Abbreviations ANS 1-anilino-naphthalene-8-sulfonate - CD circular dichroism - NMR nuclear magnetic resonance - CCA convex constraint analysis |
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| Keywords: | Chaperone SecB circular dichroism Lys oligomers conformational change |
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