ISSN:
1573-4943
Keywords:
Chaperone
;
SecB
;
circular dichroism
;
Lys oligomers
;
conformational change
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The chaperone SecB, which is involved in protein export inEscherichia coli, is shown by circular dichroism measurements to contain a high content ofβ-pleated sheets. Prediction of the secondary structure of SecB is in good agreement with the observed content ofβ-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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01886885
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