The Interaction of Proteins with Membrane Surfaces at Molecular Resolution: The Neutron Reflection Method

  • Thomas M. Bayerl
  • Andreas P. Maierhofer
Part of the Principles and Practice book series (PRINCIPLES)


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.


Neutron Beam Specular Reflection Reflectivity Curve Lipid Monolayer Extrinsic Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Bayerl TM, Thomas RK, Penfold J, Rennie AR, Sackmann E (1990) Specular reflection of neutrons at phospholipid monolayers. Changes of monolayer structure and head group hydration at the transition from the expanded to the condensed phase state. Biophys J 57:1095–1098PubMedCrossRefGoogle Scholar
  2. Behrisch A, Dietrich Ch, Noegel AA, Schleicher M, Sackmann E (1995) Actin binding protein hisactophilin binds to partially charged membranes and mediates actin coupling to membranes. Biochemistry 34:15182–15190PubMedCrossRefGoogle Scholar
  3. Born M, Wolf E (1970) Principles of optics. Pergamon Press, OxfordGoogle Scholar
  4. Brumm T, Naumann C, Sackmann E, Rennie AR, Thomas RK, Kanellas D, Penfold J, Bayerl TM (1994) Conformational changes of the lecithin head group in monolayers at the air/ water interface. A neutron reflection study. Eur Biophys J 23:289–296CrossRefGoogle Scholar
  5. Dietrich C, Goldmann WH, Sackmann E, Isenberg G (1993) Interaction of NBD — talin with lipid monolayers, a film balance study. FEBS Lett 324 /1:37–40PubMedCrossRefGoogle Scholar
  6. 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
  7. 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
  8. Johnson SJ, Bayerl TM, Weihan W, Noack H, Penfold J, Thomas RK, Kanellas D, Rennie AR, Sackmann E (1991) Coupling of spectrin and polylysine to phospholipid monolayers studied by specular reflection of neutrons. Biophys J 60:1017–1025PubMedCrossRefGoogle Scholar
  9. Kaufmann S, Käs J, Goldmann WH, Sackmann E,. Isenberg G (1992) Talin anchors and nucleates actin filaments at lipid membranes:a direct demonstration. FEBS Lett 314:203–205PubMedCrossRefGoogle Scholar
  10. Loidl-Stahlhofen A, Kaufmann S, Brumm T, Ulrich AS, Bayerl TM (1996) The thermodynamic control of protein binding to lipid bilayers for protein chromatography. Nature Biotechnol 14:999–1002CrossRefGoogle Scholar
  11. Naumann C, Dietrich C, Lu JR, Thomas RK, Rennie AR, Penfold J, Bayerl TM (1994) Structure of mixed monolayers of DPPC and polyethylene glycol monododecyl ether at the air/water interface determined by neutron reflection and film balance techniques. Langmuir 10:1919–1925CrossRefGoogle Scholar
  12. Naumann C, Brumm T, Rennie AR, Penfold J, Bayerl TM (1995) Hydration of DPPC monolayers at the air/water interface and its modulation by the nonionic surfactant C12E4:a neutron reflection study. Langmuir 11:3948–3952CrossRefGoogle Scholar
  13. Naumann C, Dietrich C, Berisch A, Bayerl T, Schleicher M, Bucknall D, Sackmann E (1996) Hisactophilin-mediated binding of actin to lipid lammelae:a neutron reflectivity study of protein membrane coupling. Biophys J 71:811–823PubMedCrossRefGoogle Scholar
  14. Penfold J, Thomas RK (1990) The apllication of the specular reflection of neutrons to the study of surfaces and interfaces. J Phys:Condensed Matter 2:1369CrossRefGoogle Scholar
  15. Russel TP (1990) X-ray and neutron reflectivity for the investigation of polymers. Material Sci Rep 5:171–271CrossRefGoogle Scholar
  16. Scheel J, Ziegelbauer K, Kupke Th, Humbel BM, Noegel AA, Gerisch G, Schleicher M (1989) Hisactophilin, a distidine-rich actin-binding protein from Dictyostelium discoideum. J Biol Chem 264 (5):2832–2839PubMedGoogle Scholar
  17. Vaknin D, Kjaer K, Ais-Nielsen J, Lösche M (1991a) Structural properties of phosphatidylcholine in a monolayer at the air/water interface. Biophys J 59:1325–1332PubMedCrossRefGoogle Scholar
  18. Vaknin D, Als-Nielsen J, Piepenstock M, Lösche M (1991b) Recognition processes at a functionalized lipid surface observed with molecular resolution. Biophys J 60:1545–1552PubMedCrossRefGoogle Scholar
  19. Vist MR, Davis JH (1990) Phase equilibria of cholesterol/DPPC mixtures:2H-NMR and DSC. Biochemistry 29:451–464PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  1. 1.Department of Biophysics, Institute for Experimental PhysicsUniversity of WürzburgWürzburgGermany

Personalised recommendations