(C) 2013 Elsevier Ltd. All rights reserved.”
“The time and space resolved characterization of laser-generated pulsed plasmas is useful not only for the comprehension of basic phenomena involved in the plasma generation and following supersonic expansion, but it also permits to control the nonequilibrium process that is useful for many applications (e.g., ion implantation). The “”on-line”"

characterization can be performed by means of Langmuir probes, ion collectors, and ion energy analyzers, in order to measure the plasma temperatures and densities of atoms, ions, and electrons. The investigated plasmas were generated by means of laser pulses with intensity of the order of 10(9) W/cm(2). The contemporary characterization of the electron (through the Langmuir selleck click here probe) and ion energy distribution functions, EEDF and IEDF, respectively, permits to correlate the ion properties, like charge states and temperatures, with the electron properties, like the shape of the EEDF at different times and distances from the ablated target surface. (C) 2010 American Institute of Physics. [doi:10.1063/1.3429242]“
“Protein loops,

the flexible short segments connecting two stable secondary structural units in proteins, play a critical role in protein structure and function. Constructing chemically sensible conformations of protein loops that seamlessly bridge the gap between the anchor points without introducing any steric collisions remains an open challenge. A variety of algorithms have been developed to tackle the loop closure problem, ranging from inverse kinematics to knowledge-based approaches that utilize pre-existing fragments extracted from known protein structures. However, many of these

approaches focus on the generation of conformations learn more that mainly satisfy the fixed end point condition, leaving the steric constraints to be resolved in subsequent post-processing steps. In the present work, we describe a simple solution that simultaneously satisfies not only the end point and steric conditions, but also chirality and planarity constraints. Starting from random initial atomic coordinates, each individual conformation is generated independently by using a simple alternating scheme of pairwise distance adjustments of randomly chosen atoms, followed by fast geometric matching of the conformationally rigid components of the constituent amino acids. The method is conceptually simple, numerically stable and computationally efficient. Very importantly, additional constraints, such as those derived from NMR experiments, hydrogen bonds or salt bridges, can be incorporated into the algorithm in a straightforward and inexpensive way, making the method ideal for solving more complex multi-loop problems.