Michael R. Morrow

TL;DR: Extensive molecular dynamics simulations together with differential scanning calorimetry (DSC) and nuclear magnetic resonance (NMR) experiments to quantify the influence of free 1,6-diphenyl-1,3,5-hexatriene (DPH) fluorescent probes on the structure and dynamics of a dipalmitoylphosphatidylcholine bilayer show that in the membrane-water interface the influence

TL;DR: Adaptation of regular solution theory to the amphiphilic peptide/1,2-bis(perdeuteriopalmitoyl)-sn-glycero-3-phosphocholine system demonstrates that the peptide concentration dependence of the transition enthalpies can be incorporated into a thermodynamic model which reproduces the observed phase behavior fairly well.

TL;DR: The ability of the protein to alter normal lipid organization was examined by using high-sensitivity differential scanning calorimetry (DSC) and 2H nuclear magnetic resonance spectroscopy (2H NMR) and studies suggest that the protein influences slow lipid motions.

TL;DR: Synthetic human pulmonary surfactant-associated protein SP-B has been interacted with chain-perdeuterated dipalmitoylphosphatidylcholine (DPPC-d62) in aqueous dispersions, and the dispersions were investigated by magnetic resonance spectroscopy.

TL;DR: It would appear that the above factors impose a tendency for the "extra" portion of the 24-carbon chain to cross the bilayer midplane where it may interact with terminal portions of acyl chains in the opposing monolayer; however, steric constraints, and probably collision events associated with lateral diffusion, induce wide orientation fluctuations in the segment involved.