We investigated the X-ray scattering signal of highly aligned multilayers of the zwitterionic lipid 1,2-dilauroyl-sn-glycero-3-phosphatidylcholine containing pores formed by the antimicrobial peptide gramicidin as a function of the peptide/lipid ratio. We are able to obtain information on the structure factor of the pore fluid, which then yields the interaction potential between pores in the plane of the bilayers. Aside from a hard core with a radius

Continuum elastic models that account for membrane thickness variations are especially useful in the description of nanoscale deformations due to the presence of membrane proteins with hydrophobic mismatch. We show that terms involving the gradient and the Laplacian of the area per lipid are significant and must be retained in the effective Hamiltonian of the membrane. We reanalyze recent numerical data, as well as experimental data on gramicidin

We study by synchrotron small-angle x-ray scattering highly aligned lamellar phases of a zwitterionic surfactant, doped with monodisperse and spherical hydrophobic inorganic particles as a function of particle concentration. Analysis of the structure factor of the two-dimensional fluid formed by the particles in the plane of the bilayer gives access to their membrane-mediated interaction, which is repulsive, with a contact value of about 4kBT and

Site directed spin labeling in combination with electron paramagnetic resonance spectroscopy has become a very effective tool for studying the dynamics and structure of biomolecules in their native environment. This work presents the basics of site directed spin labeling and provides our results obtained in spin labeling hemerythrin and hemoglobin using methanethiosulfonate spin label. Best fit magnetic and libration parameters are obtained by simulation