Solid state protein monolayers: Morphological, conformational, and functional properties

We have studied the morphological, conformational, and electron-transfer (ET) function of the metalloprotein azurin in the solid state, by a combination of physical investigation methods, namely atomic force microscopy, intrinsic fluorescence spectroscopy, and scanning tunneling microscopy. We demonstrate that a ''solid state protein film'' maintains its native-like conformation and ET function, even after removal of the aqueous solvent.