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Point-contact spectroscopy was performed on bulk samples of electron-doped high temperature superconductor Nd 2-x Ce x CuO 4-δ . The samples were characterized using X-ray diffraction and scanning electron microscopy equipped with a wavelength-dispersive spectrometer and an electron backscatter diffraction detector. Samples with Ce content x = 0.15 showed the absence of spurious phases and randomly oriented grains, most of which had dimensions of approximately 220 µm 2 . The low-bias spectra in the tunneling regime, i.e., high-transparency interface, exhibited a gap feature at about ±5 meV and no zero-bias conductance, despite the random oriented grains investigated within our bulk samples, consistent with most of the literature data on oriented samples. High-bias conductance was also measured in order to obtain information on the properties of the barrier. A V-shape was observed in some cases, instead of the parabolic behavior expected for tunnel junctions.

We performed a detailed investigation of the superconducting properties of polycrystalline Pr 1-x Ce x Pt 4 Ge 12 pellets. We report the effect of Ce substitution, for x = 0.07, on magnetic field phase diagram H-T. We demonstrate that the upper critical field is well described by the Ginzburg-Landau model and that the irreversibility field line has a scaling behaviour similar to cuprates. We also show that for magnetic fields lower than 0.4 T, the activation energy follows a power law of the type ? -1/2 , suggesting a collective pinning regime with a quasi-2D character for the Ce-doped compound with x = 0.07. Furthermore, by means of a point contact Andreev reflection spectroscopy setup, we formed metal/superconductor nano-junctions as small as tens of nanometers on the PrPt 4 Ge 12 parent compound (x = 0). Experimental results showed a wide variety of conductance features appearing in the dI/dV vs. V spectra, all explained in terms of a modified Blonder-Tinkham-Klapwijk model considering a superconducting order parameter with nodal directions as well as sign change in the momentum space for the sample with x = 0. The numerical simulations of the conductance spectra also demonstrate that s-wave pairing and anisotropic s-waves are unsuitable for reproducing experimental data obtained at low temperature on the un-doped compound. Interestingly, we show that the polycrystalline nature of the superconducting PrPt 4 Ge 12 sample can favour the formation of an inter-grain Josephson junction in series with the point contact junction in this kind of experiments.

Bovine seminal ribonuclease (BS-RNase) is the only known dimeric enzyme characterized by an equilibrium between two different 3D structures: MxM, with exchange (or swapping) of the N-terminal 1-20 residues, and M=M, without exchange. As a consequence, the hinge region 16-22 has a different tertiary structure in the two forms. In the native protein, the equilibrium ratio between MxM and M=M is about 7 : 3. Kinetic analysis of the swapping process for a recombinant sample shows that it folds mainly in the M=M form, then undergoes interconversion into the MxM form, reaching the same 7 : 3 equilibrium ratio. To investigate the role of the regions that are most affected structurally by the swapping, we expressed variant proteins by replacing two crucial residues with the corresponding ones from RNase A: Pro19, within the hinge peptide, and Leu28, located at the interface between subunits. We compared the structural properties of the monomeric forms of P19A-BS-RNase, L28Q-BS-RNase and P19A/L28Q-BS-RNase variants with those of the parent protein, and investigated the exchange kinetics of the corresponding dimers. The P19A mutation slightly increases the thermal stability of the monomer, but it does not alter the swapping tendency of the dimer. In contrast, the L28Q mutation significantly affects both the dimerization and swapping processes but not the thermal stability of the monomer. Overall, these results suggest that the structural determinants that control the exchange of N-terminal arms in BS-RNase may not be located within the hinge peptide, and point to a crucial role of the interface residues.

A series of diastereoisomers of endomorphin-1 (EM1, Tyr(1)-Pro(2)-Trp(3)-Phe(4)-NH(2)) have been synthesized and their potency measured using the guinea pig ileum assay. [D-Phe(4)]EM1 possessed 1/10 the potency of EM1, while potencies of [D-Tyr(1)]EM1 and [D-Trp(3)]EM1 were 50- and 100-fold lower, respectively. Drastic loss of activity occurred in the [D-Pro(2)]EM1 peptide. The structural determinants for the inactivity and reduced potency of the diastereoisomers were investigated using NMR spectroscopy and conformational analysis. Simulations of trans-[D-Pro(2)]EM1 using NOE-derived distance constraints afforded well-defined structures in which Tyr and Trp side chains stack against the proline ring. The inactivity of [D-Pro(2)]EM1 was explained by structural comparison with EM1 (, FEBS Lett. 439:13-20). The two peptides showed an opposite orientation of the Trp(3) residue with respect to Tyr(1), thus suggesting a role of Pro(2) as a stereochemical spacer in orienting Trp(3) and Phe(4) toward regions suitable for mu-receptor interaction. The agonist activity of [D-Tyr(1)]EM1 and [D-Trp(3)]EM1 was attributed to their ability to adopt low-energy conformations that mimic those of EM1. The requirements for mu-receptor activation were examined further by comparing EM1 with the mu-peptide [D-Ala(2), MePhe(4), Gly-ol]-enkephalin (DAMGO). Conformations of DAMGO with a Tyr(1)-MePhe(4) phenyl ring separation of approximately 12 A were found to mimic Tyr(1)-Phe(4) of EM1, thus suggesting overlapping binding modes between these two peptides.