PMID:8561855
| Citation |
Fasman, GD, Park, K and Randall, LL (1995) Chaperone SecB: conformational changes demonstrated by circular dichroism. J. Protein Chem. 14:595-600 |
|---|---|
| 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. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Circular Dichroism; Molecular Chaperones/chemistry; Protein Conformation; Protein Structure, Secondary; Sodium Chloride/administration & dosage; Sodium Chloride/pharmacology |
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