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A Verdini

Publications and source records attributed to A Verdini.

4 recordsLinked to original sources

Electronic properties of a pure and sodium-doped C(70) single layer adsorbed on Al polycrystalline surface.

Core level and valence band photoemission measurements combined with near edge x-ray absorption fine structure measurements were performed on a single C(70) layer adsorbed on polycrystalline Al (1 ML-C(70)/Al) (ML-monolayer), pure and doped with sodium atoms. The data obtained from the pure ML chemisorbed on Al surface show a semiconducting behavior of the system, which is characterized by a covalent bond between the adsorbate and the substrate. The same data show also that the C(70) molecules tend to orient themselves with the C(5v) axis perpendicular to the surface in analogy to what observed for 1 ML-C(70)/Cu(111). By doping the sample with sodium atoms a charge transfer from the alkali atoms to the lowest unoccupied molecular orbital (LUMO) of the C(70) molecules takes place, as underlined by the gradual increasing intensity of the C(70) LUMO peak as a function of doping. Nevertheless, no metallic phases are observed for any doping step.

Journal Article↗

Atomically resolved images from near node photoelectron holography experiments on Al(111).

Szöke's concept for electron holography is hampered by forward scattering that dominates electron diffraction from electron point sources below the surface top layer. Forward scattering was proposed to be suppressed if the anisotropic nature of the electron source wave is exploited [T. Greber and J. Osterwalder, Chem. Phys. Lett. 256, 653 (1996)]. Experiments show a strong suppression of forward scattering in Al(111) if Al 2s photoelectrons (E(kin) = 952 eV) are measured near the nodal plane of the outgoing p wave. The holographic reconstruction from such diffraction data provides three dimensional images of atomic sites in unit cells with a size of more than 10 A.

Journal Article↗

Solution conformation of tuftsin.

Tuftsin, a natural linear tetrapeptide (Thr-Lys-Pro-Arg) of potential antitumor activity, has been studied in DMSO-d6 solution by 2D NMR spectroscopy. 1H and 13C spectra show the presence of two families of conformations characterized by a trans or cis Lys-Pro bond, respectively. The family of conformers containing the cis peptide bond is a mixture of extended structures as expected for a short linear peptide. On the contrary, the trans isomer appears to be a rigid, folded conformer, as indicated by crucial NOEs and by the exceptionally low temperature coefficient of Arg NH. Analysis of the solution data by means of energy calculations leads to a unique structure, characterized by a Lys-Pro inverse gamma-turn.

Amino Acid Sequence↗

Poly(DL-proline), a synthetic polypeptide behaving as an ion channel across bilayer membranes.

The synthesis and characterization of poly(DL-proline) are reported in relation with its predicted property of forming ion channels across membranes. The analysis of the conductance induced in synthetic bilayer membranes doped with poly(DL-proline) shows ionic permeoselectivity and the characteristic time course of fluctuations of ion channels, according to the similarity with the active structure of gramicidin A in membranes during the ion passage. An alternative mechanism of ion transport across bilayer membranes is also advanced.

Electric Conductivity↗