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 nativelike conformation and ET function, even after removal of the aqueous solvent.
Pompa
P P
PP
National Nanotechnology Laboratories of INFM, Biomolecular Electronics Division, Department of Innovation Engineering, University of Lecce, Via per Arnesano, 73100 Lecce, Italy.
Biasco
A
A
Frascerra
V
V
Calabi
F
F
Cingolani
R
R
Rinaldi
R
R
Verbeet
M Ph
MP
de Waal
E
E
Canters
G W
GW
D000327:Adsorption; D001400:Azurin / Q000737:chemistry* / Q000648:ultrastructure*; D004579:Electron Transport; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D011485:Protein Binding; D011487:Protein Conformation; D012997:Solvents / Q000737:chemistry*; D013329:Structure-Activity Relationship; D014867:Water / Q000737:chemistry*
D046912:Multiprotein Complexes; D012997:Solvents; D014867:Water; D001400:Azurin