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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Bibliographic Details
Published inJournal of protein chemistry Vol. 14; no. 7; p. 595
Main Authors Fasman, G D, Park, K, Randall, L L
Format Journal Article
LanguageEnglish
Published United States 01.10.1995
Subjects
Bacterial Proteins - chemistry
Circular Dichroism
Molecular Chaperones - chemistry
Protein Conformation
Protein Structure, Secondary
Sodium Chloride - administration & dosage
Sodium Chloride - pharmacology
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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.
ISSN:0277-8033
DOI:10.1007/BF01886885