The Interaction of Proteins with Membrane Surfaces at Molecular Resolution: The Neutron Reflection Method
Neutron scattering represents a unique tool for studying the structure and the phase behavior of lipid membranes. Among the latest applications of neutron scattering in lipid membranes is the neutron reflection technique. This method proves as very powerful for the study of the interfacial structure of lipid monolayers at the air-water interface and its changes due to the presence of water-soluble proteins. Moreover, its sample quantity requirements are extremely low compared to other neutron techniques, is generally in the microgram to milligram region. This makes it suitable for the neutron study of rare and expensive biological macromolecules. A particularly interesting feature of this method from the cell biology point of view is that it allows the acquisition of information about the penetration depth of extrinsic proteins into the monolayer and the associated changes of the lipid head group hydration. After giving an introduction into neutron reflection theory and the experimental setup, we will concentrate on this biological aspect by discussing results obtained from the study of monolayer interaction with different extrinsic proteins.
KeywordsSurfactant Chrome Hydrocarbon Glycol Syringe
Unable to display preview. Download preview PDF.
- Born M, Wolf E (1970) Principles of optics. Pergamon Press, OxfordGoogle Scholar
- Habazettl J, Gondol D, Wiltscheck R, Otlewski J, Schleicher M, T. Holak A (1992) Structure of hisactophilin is similar to interleukin-1b and fibroblast growth factor. Nature 359:855–858Google Scholar
- Hanakam F, Eckerskorn C, Lottspeich F, Müller-Taubenberger A, Schäfer W, Gerisch G (1995) The pH-sensitive actin-binding protein hisactophilin of Dictyostelium exists in two isoforms which both are myristylated and distributed between plasma membrane and cytoplasm. J Biol Chem 270:596–602PubMedCrossRefGoogle Scholar