Adiabatic Dynamics of Superconducting Quantum Point Contacts

Starting from the quasiclassical equations for non-equilibrium Green's functions we derive a simple kinetic equation that governs ac Josephson effect in a superconducting quantum point contact at small bias voltages. In contrast to existing approaches the kinetic equation is valid for voltages with arbitrary time dependence. We use this equation to calculate frequency-dependent linear conductance, and dc $I\!-\!V$ characteristics with and without microwave radiation for resistively shunted quantum point contacts. A novel feature of the $I\!-\!V$ characteristics is the excess current $2I_c/\pi$ appearing at small voltages. An important by-product of our derivation is the analytical proof that the microscopic expression for the current coincides at arbitrary voltages with the expression that follows from the Bogolyubov-de Gennes equations, if one uses appropriate amplitudes of Andreev reflection which contain information about microscopic structure of the superconductors.Comment: 12 Pages, REVTEX 3.0, 3 figures available upon reques

Josephson currents through spin-active interfaces

The Josephson coupling of two isotropic s-wave superconductors through a small, magnetically active junction is studied. This is done as a function of junction transparency and of the degree of spin-mixing occurring in the barrier. In the tunneling limit, the critical current shows an anomalous 1/T temperature dependence at low temperatures and for certain magnetic realizations of the junction. The behavior of the Josephson current is governed by Andreev bound states appearing within the superconducting gap and the position of these states in energy is tunable with the magnetic properties of the barrier. This study is done using the equilibrium part of the quasiclassical Zaitsev-Millis-Rainer-Sauls boundary condition for spin-active interfaces and a general solution of the boundary condition is found. This solution is a generalization of the one recently presented by Eschrig [M. Eschrig, Phys. Rev B 61, 9061 (2000)] for spin-conserving interfaces and allows an effective treatment of the problem of a superconductor in proximity to a magnetically active material.Comment: 8 pages + 3 eps figure

Fused eco29kIR- and M genes coding for a fully functional hybrid polypeptide as a model of molecular evolution of restriction-modification systems

<p>Abstract</p> <p>Background</p> <p>The discovery of restriction endonucleases and modification DNA methyltransferases, key instruments of genetic engineering, opened a new era of molecular biology through development of the recombinant DNA technology. Today, the number of potential proteins assigned to type II restriction enzymes alone is beyond 6000, which probably reflects the high diversity of evolutionary pathways. Here we present experimental evidence that a new type IIC restriction and modification enzymes carrying both activities in a single polypeptide could result from fusion of the appropriate genes from preexisting bipartite restriction-modification systems.</p> <p>Results</p> <p>Fusion of <it>eco29kIR </it>and <it>M </it>ORFs gave a novel gene encoding for a fully functional hybrid polypeptide that carried both restriction endonuclease and DNA methyltransferase activities. It has been placed into a subclass of type II restriction and modification enzymes - type IIC. Its MTase activity, 80% that of the M.Eco29kI enzyme, remained almost unchanged, while its REase activity decreased by three times, concurrently with changed reaction optima, which presumably can be caused by increased steric hindrance in interaction with the substrate. <it>In vitro </it>the enzyme preferentially cuts DNA, with only a low level of DNA modification detected. <it>In vivo </it>new RMS can provide a 10²-fold less protection of host cells against phage invasion.</p> <p>Conclusions</p> <p>We propose a molecular mechanism of appearing of type IIC restriction-modification and M.SsoII-related enzymes, as well as other multifunctional proteins. As shown, gene fusion could play an important role in evolution of restriction-modification systems and be responsible for the enzyme subclass interconversion. Based on the proposed approach, hundreds of new type IIC enzymes can be generated using head-to-tail oriented type I, II, and III restriction and modification genes. These bifunctional polypeptides can serve a basis for enzymes with altered recognition specificities. Lastly, this study demonstrates that protein fusion may change biochemical properties of the involved enzymes, thus giving a starting point for their further evolutionary divergence.</p