Bonca and S. A. Trugman, Phys. Rev. Lett. 75, 2566 (1995)]. In both approaches, thermal relaxation in the nuclear subspace is implemented in equivalent approximate ways: In the Ehrenfest calculation the uncoupled (to the electronic subsystem) motion of the classical (harmonic) oscillator is simply damped as would be implied by coupling ARN-509 ic50 to a Markovian zero temperature bath. In the quantum calculation, thermal relaxation is implemented by augmenting the Liouville

equation for the oscillator density matrix with kinetic terms that account for the same relaxation. In both cases we calculate the probability to trap the electron by forming a polaron and the probability that it escapes to infinity. Comparing

these calculations, we find that while both result in similar long time yields for these processes, the Ehrenfest-dynamics based calculation fails to account for the correct time scale for the polaron formation. This failure results, as usual, from the fact that at the early stage of polaron formation the classical nuclear dynamics takes place on an unphysical average potential surface that reflects the distributed electronic population in the system, while the quantum calculation accounts fully for correlations between the electronic and vibrational subsystems. (C) 2013 American Institute of Physics. [http://dx.doi.org/10.1063/1.4776230]“
“Surface proteins consist of secreted and membrane proteins and play a central role in the interaction of the pathogen SC79 with its environment, especially in the pathogenicity of Mycobacterium tuberculosis (MTB). Research on surface proteins in MTB has focused on 2D electrophoresis of culture filtrate proteins (CFP), extraction of transmembrane proteins with detergent and predicting their properties with a range of available algorithms. However, functional analysis of these secretomes is possible only if many proteins are AZD1775 expressed

and purified individually, which limits a large number of studies to the function of the proteome. Here, we utilized a phage display system to construct a whole genomic surface protein phage display library of MTB, which can complete direct selection, identification, expression, purification and functional research of surface proteins of MTB. With this system we made a new serological approach involving iterative subtraction screening. Cross-reactivity of antibodies was reduced by preadsorption of the surface protein phage display library with the sera of healthy BCG-vaccinated individuals prior to studying their reactivity against the sera of tuberculosis (TB) patients. As a result six antigens were identified, three of which have not previously been reported as diagnosis antigens. The surface protein phage display library shows great promise in the study of MTB. (C) 2011 Elsevier Ltd. All rights reserved.