Self‐Association of Unfolded Outer Membrane Proteins

Macromolecular Bioscience - Tập 10 Số 7 - Trang 763-767 - 2010
Alexandra Ebie Tan1, N. K. Burgess2, Diana S. DeAndrade2, Jacob D. Marold2, Karen G. Fleming3
1Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA
2Department of Biophysics, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA
3Department of Biophysics, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA. Fax: (+1) 410 516 4118

Tóm tắt

AbstractWe have investigated self‐association propensities of aqueous unfolded (UAQ) forms of eight outer membrane proteins (OMPs), OmpA, OmpW, OmpX, PagP, OmpT, OmpLa, FadL, and Omp85. We found that high urea concentrations maintain all of these OMPs as monomers and that OmpA and OmpX remain monomeric upon dilution to 1 M urea. A pH screen showed that basic pH supports the least amount of UAQ OMP self‐association, consistent with earlier studies showing that basic pH was optimal for better folding efficiencies. The addition of KCl increased UAQ OMP self‐association, although the magnitudes of the responses were varied. These studies showed that urea can be used to tune the amount of UAQ OMP self‐association and indicate that the presence of some urea may be useful in optimizing folding conditions because it diminishes aggregation.magnified image

Từ khóa


Tài liệu tham khảo

10.1126/science.1143993

10.1073/pnas.0701579104

10.1007/BF01868635

10.1016/j.cell.2005.02.015

10.1093/emboj/20.1.285

10.1074/jbc.M802754200

10.1074/jbc.M100464200

10.1016/j.jmb.2007.07.072

10.1016/j.chemphyslip.2006.02.004

10.1021/bi982465w

10.1110/ps.8.10.2065

10.1046/j.1365-2958.1996.561412.x

10.1074/jbc.274.35.24567

10.1016/j.bpc.2003.10.028

10.1016/j.ab.2006.04.053

10.1016/S0006-3495(00)76713-0

Laue T. M., 1992, Analytical Ultracentrifugation in Biochemistry and Polymer Science, 90

Cohn E. J., 1943, Proteins, Amino Acids and Peptides, 370

10.1073/pnas.89.16.7457

Thông tin
Thông tin xuất bản

Macromolecular Bioscience

Tập 10 Số 7

763-767

Thông tin tác giả