'Electron paramagnetic resonance spectra simulation directly from molecular dynamics trajectories of a liquid crystal with a doped paramagnetic spin probe.', Physical review letters., 102 (1). 013005. Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details.

Liquid crystals spin their secrets: Electron paramagnetic resonance (EPR) spectra are predicted directly and completely from fully atomistic molecular dynamics (MD) simulations of 4-cyano-4-n-pentylbiphenyl (5CB) nematic liquid crystals with a doped nitroxide spin probe (depicted in yellow; red curve = simulated and blue curve = measured EPR spectrum).

Biophysical studies of model cell membranes at full and low hydration are usually carried out using scattering measurements on multi-bilayer systems. Molecular simulations of lipid bilayers aimed at reproducing those experimental conditions are usually conducted using single bilayers with different amounts of water. These simulation conditions may lead to artifacts arising from size effects and self-interactions because of periodic boundary conditions. We have tested the influence of the size and number of bilayers on membrane properties using the Lipid14 force field for lipids in molecular dynamics simulations of 1,2-dioleoyl-sn-glycero-3-phosphocholine bilayers at full hydration (44 water molecules per lipid), low hydration (18 water molecules per lipid), and dehydration (9 water molecules per lipid). A number of additional simulations were conducted with the Slipids force field for comparison. We have found that the average area per lipid (APL), thickness, mass density profiles, and acyl tail order parameters are insensitive to the size and the number of bilayers for all hydration states. The Lipid14 force field can also successfully reproduce the experimentally observed decrease in APL and corresponding increase in bilayer thickness upon dehydration, reflecting the increase in ordering as the system becomes more gel-like. Additionally, decreasing hydration levels were associated with a trend away from normal lateral diffusion and toward more subdiffusive regimes across both force fields. In summary, at least for the Lipid14 force field, the use of a single bilayer with 128 phospholipid molecules provides an adequate representation of multi-bilayer systems at varying levels of hydration.

We report the prediction of motional EPR spectra of the metalloprotein sperm whale myoglobin spin labelled with nitroxide directly from Molecular Dynamics (MD) simulations at the atomistic scale. We show that an accurate simulation of EPR spectra can be achieved from a single MD trajectory which is in excellent agreement with experiment. Simulations have been carried out using a general method reported previously by us for the simulation of EPR spectra form single dynamical trajectories. Our calculations demonstrate the complex nature of the dynamics of a spin label which is a superposition of the fast librational motions around dihedral states, of slow conformational flips among different rotameric states and of the slow rotational diffusion of the protein itself. The MD-EPR methodology reported does not require any additional stochastic modelling using adjustable parameters and opens, for the first time, the prospect of the simulation of EPR spectra entirely from single MD trajectories. Such a technique not only simplifies the interpretation and analysis of EPR spectra but also opens the possibility, for example, of "computer engineering" of spin-labelled proteins with the desired properties prior to actual EPR experiment.

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