Chaperone SecB: Conformational Changes Demonstrated by Circular Dichroism

Overview

Journal J Protein Chem

Specialties Biochemistry
Chemistry

Date 1995 Oct 1

PMID 8561855

Citations 3

Authors

G D Fasman

K Park

L L Randall

Affiliations

Soon will be listed here.

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.

Citing Articles

Biophysical characterization of the influence of salt on tetrameric SecB.

Dekker C, Agianian B, Weik M, Zaccai G, Kroon J, Gros P Biophys J. 2001; 81(1):455-62.

PMID: 11423428 PMC: 1301525. DOI: 10.1016/S0006-3495(01)75713-X.

Protein targeting to the bacterial cytoplasmic membrane.

Fekkes P, Driessen A Microbiol Mol Biol Rev. 1999; 63(1):161-73.

PMID: 10066835 PMC: 98961. DOI: 10.1128/MMBR.63.1.161-173.1999.

Electrospray mass spectrometric investigation of the chaperone SecB.

Smith V, Schwartz B, Randall L, Smith R Protein Sci. 1996; 5(3):488-94.

PMID: 8868485 PMC: 2143373. DOI: 10.1002/pro.5560050310.

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