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 demon...

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Bibliographic Details
Published in:The Journal of chemical physics 2004-12, Vol.121 (21), p.10325-10328
Main Authors: Pompa, P P, Biasco, A, Frascerra, V, Calabi, F, Cingolani, R, Rinaldi, R, Verbeet, M Ph, de Waal, E, Canters, G W
Format: Article
Language:English
Subjects:
Adsorption
Azurin - chemistry
Azurin - ultrastructure
Electron Transport
Multiprotein Complexes - chemistry
Multiprotein Complexes - ultrastructure
Protein Binding
Protein Conformation
Solvents - chemistry
Structure-Activity Relationship
Water - chemistry
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Summary: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.
ISSN:0021-9606
1089-7690
DOI:10.1063/1.1828038