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 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.
Fasman
G D
GD
Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254, USA.
Park
K
K
Randall
L L
LL
D001426:Bacterial Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D018832:Molecular Chaperones / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012965:Sodium Chloride / Q000008:administration & dosage / Q000494:pharmacology
D001426:Bacterial Proteins; D018832:Molecular Chaperones; C057842:SecB protein, Bacteria; D012965:Sodium Chloride