Format

Send to

Choose Destination
Biochemistry. 2006 Jul 18;45(28):8453-65.

Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins.

Author information

1
Department of Chemistry, University of Toronto, UTM, 3359 Mississauga Road, North Mississauga, ON, Canada L5L 1C6. sprosser@utm.utoronto.ca

Abstract

This review covers current trends in studies of membrane amphiphiles and membrane proteins using both fast tumbling bicelles and magnetically aligned bicelle media for both solution state and solid state NMR. The fast tumbling bicelles provide a versatile biologically mimetic membrane model, which in many cases is preferable to micelles, both because of the range of lipids and amphiphiles that may be combined and because radius of curvature effects and strain effects common with micelles may be avoided. Drug and small molecule binding and partitioning studies should benefit from their application in fast tumbling bicelles, tailored to mimic specific membranes. A wide range of topology and immersion depth studies have been shown to be effective in fast tumbling bicelles, while residual dipolar couplings add another dimension to structure refinement possibilities, particularly for situations in which the peptide is uniformly labeled with 15N and 13C. Solid state NMR studies of polytopic transmembrane proteins demonstrate that it is possible to express, purify, and reconstitute membrane proteins, ranging in size from single transmembrane domains to seven-transmembrane GPCRs, into bicelles. The line widths and quality of the resulting 15NH dipole-15N chemical shift spectra demonstrate that there are no insurmountable obstacles to the study of large membrane proteins in magnetically aligned media.

PMID:
16834319
DOI:
10.1021/bi060615u
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for American Chemical Society
Loading ...
Support Center