Bicelles as model membranes for solid‐ and solution‐state NMR studies of membrane peptides and proteins
Authors:
- 26 January 2005
- journal article
- research article
- Published by Wiley in Concepts in Magnetic Resonance Part A
- Vol. 24A (1) , 17-37
Abstract
Bicelles are an attractive membrane mimetic system because of their planar surface and lipid composition, which resemble biological membranes. In addition, their orientation and morphologic properties make them amenable to solid‐ and solution‐state NMR. This article reviews the physical properties of bicelles, such as magnetic alignment and viscosity as well as the different models proposed in the literature to explain the bicelle morphology. The utility of bicelles for studying the interaction and structure of membrane peptides and proteins by solid‐ and solution‐state NMR is also presented, along with the advantages and limitations of bicelles. © 2005 Wiley Periodicals, Inc. Concepts Magn Reson Part A 24A: 17–37, 2005.Keywords
This publication has 122 references indexed in Scilit:
- NMR solution structure and position of transportan in neutral phospholipid bicellesFEBS Letters, 2004
- NMR Structure of the Integral Membrane Protein OmpXJournal of Molecular Biology, 2004
- Using Sodium Cation Organization To Study the Phase Behavior of Bicelle SolutionsThe Journal of Physical Chemistry B, 2003
- Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structureJournal of Molecular Biology, 2002
- Measurement of Residual Dipolar Couplings of Macromolecules Aligned in the Nematic Phase of a Colloidal Suspension of Rod-Shaped VirusesJournal of the American Chemical Society, 1998
- Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues 1 † 1Edited by P. E. Wright †The coordinates of the 25 structures of the protein in both micellar systems have been deposited with the Brookhaven Protein Data Bank, along with the related NMR constraints. Entry codes are 2CPB, R2CPBMR (DodPCho) and 2CPS, R2CPSMR (SDS), respectively.Journal of Molecular Biology, 1998
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- 2H NMR lineshapes of immobilized uniaxially oriented membrane proteinsSolid State Nuclear Magnetic Resonance, 1993
- Conformational studies of lipid-bound polypeptides by elucidation of proton-proton cross-relaxation networksBiochemical and Biophysical Research Communications, 1980
- 31P nuclear magnetic resonance and the head group structure of phospholipids in membranesBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1978