Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.
 

Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.

Related Articles Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.

Biochim Biophys Acta. 2014 Jun 16;

Authors: Kinnun JJ, Mallikarjunaiah KJ, Petrache HI, Brown MF

Abstract
This article reviews the application of solid-state (2)H nuclear magnetic resonance (NMR) spectroscopy for investigating the deformation of lipid bilayers at the atomistic level. For liquid-crystalline membranes, the average structure is manifested by the segmental order parameters (SCD) of the lipids. Solid-state (2)H NMR yields observables directly related to the stress field of the lipid bilayer. The extent to which lipid bilayers are deformed by osmotic pressure is integral to how lipid-protein interactions affect membrane functions. Calculations of the average area per lipid and related structural properties are pertinent to bilayer remodeling and molecular dynamics (MD) simulations of membranes. To establish structural quantities, such as area per lipid and volumetric bilayer thickness, a mean-torque analysis of (2)H NMR order parameters is applied. Osmotic stress is introduced by adding polymer solutions or by gravimetric dehydration, which are thermodynamically equivalent. Solid-state NMR studies of lipids under osmotic stress probe membrane interactions involving collective bilayer undulations, order-director fluctuations, and lipid molecular protrusions. Removal of water yields a reduction of the mean area per lipid, with a corresponding increase in volumetric bilayer thickness, by up to 20% in the liquid-crystalline state. Hydrophobic mismatch can shift protein states involving mechanosensation, transport, and molecular recognition by G-protein-coupled receptors. Measurements of the order parameters versus osmotic pressure yield the elastic area compressibility modulus and the corresponding bilayer thickness at an atomistic level. Solid-state (2)H NMR thus reveals how membrane deformation can affect protein conformational changes within the stress field of the lipid bilayer. This article is part of a Special Issue entitled: NMR Spectroscopy for Atomistic Views of Biomembranes and Cell Surfaces.


PMID: 24946141 [PubMed - as supplied by publisher]



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