Sea-quark flavor asymmetry in the nucleon from a relativistic analysis of the Drell-Yan scattering off nuclei

It is shown that accounting for the relativistic structure of the deuteron allows to explain the ratio of the Drell-Yan pair production cross-section at the low Bjorken $x$ off the deuteron and the proton. Thus, the sea quark distributions in the nucleon should be studied with accounting for the effects of the relativistic structure of the deuteron. The suggested approach reduces theoretical uncertainty in extracting the ratio $\bar u/\bar d$ from the data and it is important for the clarification of the nature of the sea quark asymmetry in the nucleon.Comment: 4 pages, 1 figures, Chiral Symmetry in Hadron and Nuclear Physics November 13-16, 2007, Osak

Gauge symmetries and structure of proteins

We discuss the gauge field theory approach to protein structure study, which allows a natural way to introduce collective degrees of freedom and nonlinear topological structures. Local symmetry of proteins and its breaking in the medium is considered, what allows to derive Abelian Higgs model of protein backbone, correct folding of which is defined by gauge symmetry breaking due hydrophobic forces. Within this model structure of protein backbone is defined by superposition of one-dimensional topological solitons (kinks), what allows to reproduce the three-dimensional structure of the protein backbone with precision up to 1A and to predict its dynamics

Vortices in

We discuss the properties of the non-Hermitian -symmetric two–scalar fields model. We investigate stability areas of this system and properties of vortices that emerge in the system of two interacting scalar fields. The phase diagram of the model contains stable and unstable regions depending on -symmetry breaking, which intercross the regions of U(1)-symmetric and U(1)-broken phases in a nontrivial way. At non-zero quartic couplings, the non-Hermitian model possesses classical vortex solutions in the -symmetric regions. We also consider a close Hermitian analog of the theory and compare the results with the non-Hermitian model

On topology and knotty entanglement in protein folding.

We investigate aspects of topology in protein folding. For this we numerically simulate the temperature driven folding and unfolding of the slipknotted archaeal virus protein AFV3-109. Due to knottiness the (un)folding is a topological process, it engages the entire backbone in a collective fashion. Accordingly we introduce a topological approach to model the process. Our simulations reveal that the (un)folding of AFV3-109 slipknot proceeds through a folding intermediate that has the topology of a trefoil knot. We observe that the final slipknot causes a slight swelling of the folded AFV3-109 structure. We disclose the relative stability of the strands and helices during both the folding and unfolding processes. We confirm results from previous studies that pointed out that it can be very demanding to simulate the formation of knotty self-entanglement, and we explain how the problems are circumvented: The slipknotted AFV3-109 protein is a very slow folder with a topologically demanding pathway, which needs to be properly accounted for in a simulation description. When we either increase the relative stiffness of bending, or when we decrease the speed of ambient cooling, the rate of slipknot formation rapidly increases