Solid state protein monolayers: Morphological, conformational, and functional properties (Articolo in rivista)

Type
Label
  • Solid state protein monolayers: Morphological, conformational, and functional properties (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1063/1.1828038 (literal)
Alternative label
  • Pompa, P.P; Biasco, A.; Frascerra, V.; Calabi, F.; Cingolani, R.; Rinaldi, R.; Verbeet, M.R.; De Waal, E.; Canters, G.W. (2004)
    Solid state protein monolayers: Morphological, conformational, and functional properties
    in The Journal of chemical physics
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Pompa, P.P; Biasco, A.; Frascerra, V.; Calabi, F.; Cingolani, R.; Rinaldi, R.; Verbeet, M.R.; De Waal, E.; Canters, G.W. (literal)
Pagina inizio
  • 10325 (literal)
Pagina fine
  • 10328 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://onlinelibrary.wiley.com/doi/10.1002/adma.200400628/abstract (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 121 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 4 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 21 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Natl. Nanotechnology Labs. of INFM, Biomolecular Electronics Division, University of Lecce, Via per Arnesano, 73100 Lecce, Italy Gorlaeus Laboratoria, Leiden University, Leiden, Netherlands (literal)
Titolo
  • Solid state protein monolayers: Morphological, conformational, and functional properties (literal)
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. (literal)
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