Biological activities of integral membrane proteins depend on the nature of the surrounding lipid bilayer [1]. The dynamic organization of lipid bilayer systems spans a wide frequency range encompassing individual fast acyl motions, molecular rotations, lipid protrusions, and collective bilayer fluctuations [2]. Time scales of these motional modes typically span a large range from sub-picoseconds up to milliseconds, and can be investigated using solid-state NMR spectroscopy. To correlate structural changes of lipid bilayers mediated by osmotic stress [3] with biological function and molecular dynamics, we measured 2H longitudinal (R1Z) and transverse (R2CP) relaxation rates in the liquid-crystalline phase of DMPC-d54 membrane bilayers at various hydration levels. The R1Z experiments used a conventional inversion-recovery pulse sequence, while R2CP rates were measured from quadrupolar-echo intensities using a Carr-Purcell-Meiboom-Gill pulse train. By Fourier transforming individual echoes with different pulse spacings we map the frequency dependence of relaxation rates and motional modes of individual acyl segments. Empirical correlations of acyl chain segmental order parameters (SCD) and R1Zprofiles followed a theoretical square-law functional dependence [4]. Our preliminary results show that R2CP is sensitive to hydration levels as well as the acyl position, thus indicating the presence of slow dynamic modes. The R2CPrates of the acyl segments near the polar head groups increase with lipid dehydration, while the acyl segments deeper in the hydrophobic region show lower R2CP values at high dehydration levels. Similar studies in presence of peptides and proteins can give insight into optimized lipid hydration for protein functionality and slow cooperative motions.[1] M.F. Brown (1994) Chem. Phys. Lipids 73, 159–180.[2] A. Leftin et al. (2011) Biochim. Biophys. Acta 1808, 818–839.[3] K.J. Mallikarjunaiah et al. (2011) Biophys. J. 100, 98–107.[4] M.F. Brown (1982) J. Chem. Phys. 77, 1576–1599.
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