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Infrared spectroscopy of proteins and peptides in lipid bilayers.
The application of infrared spectroscopy to the static and dynamic structure of proteins and peptides in lipid bilayers is reviewed and limitations of the technique with regard to the absolute determination of secondary structure and orientation are discussed. Expand
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
We have determined the three-dimensional fold of the 19 kDa (177 residues) transmembrane domain of the outer membrane protein A of Escherichia coli in dodecylphosphocholine (DPC) micelles in solutionExpand
Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
The N-terminal domain of the influenza hemagglutinin is deduced to be a kinked, predominantly helical amphipathic structure that could perturb lipid packing and facilitate lipid mixing between juxtaposed membranes. Expand
Folding and assembly of β-barrel membrane proteins
The stability of β-barrel membrane proteins in membranes is not as large as previously thought and is modulated by elastic forces of the lipid bilayer. Expand
Supported phospholipid bilayers.
Lateral diffusion measurements of L-alpha-dipalmitoylphosphatidylcholine (DPPC) bilayers supported on oxidized silicon wafers reveal two sharp phase transitions at temperatures similar to those found in multilayer systems with several different techniques. Expand
Reversible and Irreversible Adhesion of Motile Escherichia coli Cells Analyzed by Total Internal Reflection Aqueous Fluorescence Microscopy
It is proposed that the “force” holding swimming cells near the surface is actually the result of a hydrodynamic effect, causing the cells to swim at an angle along the glass, and that DLVO-type forces are responsible only for the observed immobilization of irreversibly adhering cells. Expand
Tethered polymer-supported planar lipid bilayers for reconstitution of integral membrane proteins: silane-polyethyleneglycol-lipid as a cushion and covalent linker.
A new tethered polymer-supported planar lipid bilayer system was developed, which permitted us to reconstitute integral membrane proteins in a laterally mobile form and a model for the interaction of these proteins with the underlying polymer is discussed. Expand
Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation
NMR data for full-length synaptobrevin in dodecylphosphocholine micelles reveals two transient helical segments flanked by natively disordered regions and a third more stable helix that may have important consequences for SNARE complex folding and fusion. Expand
Formation of supported planar bilayers by fusion of vesicles to supported phospholipid monolayers.
The lateral diffusion experiments confirm that continuous extended bilayers are formed by the monolayer-fusion technique, independent of the method by which the bilayers were prepared. Expand
Folding intermediates of a beta-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism.
A simple folding model for beta-barrel membrane proteins is presented, in which folding and membrane insertion are coupled processes which involve at least four kinetically distinguishable steps and both membrane-bound intermediates can be stabilized in fluid lipid bilayers at low temperatures. Expand