NDLI: Reconstitution and alignment by a magnetic field of a β-barrel membrane protein in bicelles

Content Provider	Springer Nature Link
Author	Triba, Mohamed N. Zoonens, Manuela Popot, Jean Luc Devaux, Philippe F. Warschawski, Dror E.
Copyright Year	2005
Abstract	A protocol is described for the reconstitution of a transmembrane β-barrel protein domain, tOmpA, into lipid bicelles. tOmpA is the largest protein to be reconstituted in bicelles to date. Its insertion does not prevent bicelles from orienting with their plane either parallel or perpendicular to the magnetic field, depending on the absence or presence of paramagnetic ions. In the latter case, tOmpA is shown to align with the axis of the β-barrel parallel to the magnetic field, i.e. perpendicular to the plane of the bilayer, an orientation conforming to that in natural membranes and favourable to structural studies by solid-state NMR. Reconstitution into bicelles may offer an interesting approach for structural studies of membrane proteins in a medium resembling a biological membrane, using either NMR or other biophysical techniques. Our data suggest that alignment in the magnetic field of membrane proteins included into bicelles may be facilitated if the protein is folded as a β-barrel structure.
Starting Page	268
Ending Page	275
Page Count	8
File Format	PDF
ISSN	01757571
Journal	European Biophysics Journal
Volume Number	35
Issue Number	3
e-ISSN	14321017
Language	English
Publisher	Springer-Verlag
Publisher Date	2005-09-27
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Solid-state NMR Membrane protein Bicelle Outer membrane protein A (OmpA) Structure Orientation Neurobiology Animal Physiology Plant Physiology Biochemistry Cell Biology Biophysics/Biomedical Physics
Content Type	Text
Resource Type	Article
Subject	Medicine Biophysics

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