Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure.
In this review we discuss the use of X-ray and neutron diffraction methods for investigating the temperature- and pressure-dependent structure and phase behaviour of lipid and model biomembrane systems. Hydrostatic pressure has been used as a physical parameter for studying the stability and energetics of lipid mesophases, but also because high pressure is an important feature of certain natural membrane environments and because the high pressure phase behaviour of biomolecules is of importance for several biotechnological processes. Using the pressure jump relaxation technique in combination with time-resolved synchrotron X-ray diffraction, the kinetics of different lipid phase transformations was investigated. The techniques can also be applied to the study of other soft matter and biomolecular phase transformations, such as surfactant phase transitions and protein un/refolding reactions. Several examples are given. In particular, we present data on the pressure-induced unfolding and refolding of small proteins, such as Snase. The data are compared with the corresponding results obtained using other trigger mechanisms and are discussed in the light of recent theoretical approaches.
Winter
Roland
R
Department of Chemistry, Physical Chemistry I, University of Dortmund, Dortmund, Germany. winter@steak.chemie.uni-dortmund.de
D002462:Cell Membrane / Q000737:chemistry; D006801:Humans; D008563:Membrane Lipids / Q000032:analysis*; D009502:Neutrons; D011312:Pressure; D011506:Proteins / Q000032:analysis*; D012996:Solutions; D017356:Synchrotrons; D014961:X-Ray Diffraction / Q000379:methods
D008563:Membrane Lipids; D011506:Proteins; D012996:Solutions