| Abstract
| - The surface shear viscosity of a myelin mimetic Langmuir monolayer is investigated upon adsorption ofmyelin basic protein (MBP). We measure an increase of the surface shear viscosity at picomolar concentrationsof the protein, suggesting that the globular conformation of MBP changes upon adsorption at the monolayer.The conformational change enables hydrodynamic interactions of the proteins, with a typical separation ofhundreds of nanometers. This unfolding is essential for the compactification of the myelin sheath, serving anenhanced saltatory signal transduction in vertebrates. The viscometry used extends the sensitivity of standardsurface viscometers toward lower viscosities.
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