Aufsatz in einer Fachzeitschrift


Refolding of outer membrane protein A in neutral or zwitterlonic detergents requires micelles and does not depend on the detailed chemical structure of the detergent






Details zur Publikation
Autor(inn)en:
Kleinschmidt, J.; Wiener, C.; Tamm, L.
Publikationsjahr:
1999
Zeitschrift:
Biophysical Journal
Seitenbereich:
A106
Abkürzung der Fachzeitschrift:
Biophys. J.
Jahrgang/Band:
76
Heftnummer:
1
ISSN:
0006-3495
eISSN:
1542-0086

Zusammenfassung, Abstract


Outer membrane protein A (OmpA) of E. coli is an integral membrane protein of the β-barrel type which becomes completely unfolded in 8 M urea in the absence of detergent. The protein refolds into detergent micelles or lipid bilayers upon rapid dilution of the denaturant. In this study, we sought to determine optimal conditions for refolding and insertion of OmpA into different detergents. Refolding studies were carried out using a range of non-ionic detergents with different headgroups and hydrophobic chain lengths. We found that a compact tertiary structure was only formed close to or above the critical micelle concentration (CMC), but not in monomeric detergent solutions. Above the CMC, refolding of OmpA was independent of the polar headgroup and hydrophobic chain length of all neutral or zwitterionic detergents that were examined. The formation of secondary structure also correlated with the formation of micelles of short chain phospholipids. It is concluded that OmpA requires for refolding a preformed aggregated lipid substrate rather than recruiting monomeric lipid on its newly formed hydrophobic perimeter.



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