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.

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

Calabi F;
2004

Abstract

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.
2004
Istituto di Nanotecnologia - NANOTEC
Istituto Nanoscienze - NANO
Metalloprotein
Atomic Force Microscopy
Scanning Probe Microscopy
Intrinsic protein fluorescence spectroscopy
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/633
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