Browsing by Author "Mallikarjunaiah, K. J."

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    Correction: Flexible lipid nanomaterials studied by NMR spectroscopy
    (Royal Society of Chemistry, 2021) Mallikarjunaiah, K. J.; Kinnun, Jacob J.; Petrache, Horia I.; Brown, Michael F.; Physics, School of Science
    The authors would like to add an additional acknowledgement to NIH Grant R01EY026041 and NSF grant MCB-1817862. The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.
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    Elastic deformation and area per lipid of membranes: atomistic view from solid-state deuterium NMR spectroscopy
    (Elsevier, 2015-01) Kinnun, Jacob A.; Mallikarjunaiah, K. J.; Petrache, Horia I.; Brown, Michael F.; Department of Physics, School of Science
    This article reviews the application of solid-state ²H 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 ²H 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 ²H 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 ²H NMR thus reveals how membrane deformation can affect protein conformational changes within the stress field of the lipid bilayer.