25,450 research outputs found
Adsorption of Self-Assembled Rigid Rods on Two-Dimensional Lattices
Monte Carlo (MC) simulations have been carried out to study the adsorption on
square and triangular lattices of particles with two bonding sites that, by
decreasing temperature or increasing density, polymerize reversibly into chains
with a discrete number of allowed directions and, at the same time, undergo a
continuous isotropic-nematic (IN) transition. The process has been monitored by
following the behavior of the adsorption isotherms for different values of
lateral interaction energy/temperature. The numerical data were compared with
mean-field analytical predictions and exact functions for noninteracting and 1D
systems. The obtained results revealed the existence of three adsorption
regimes in temperature. (1) At high temperatures, above the critical one
characterizing the IN transition at full coverage Tc(\theta=1), the particles
are distributed at random on the surface and the adlayer behaves as a
noninteracting 2D system. (2) At very low temperatures, the asymmetric monomers
adsorb forming chains over almost the entire range of coverage, and the
adsorption process behaves as a 1D problem. (3) In the intermediate regime, the
system exhibits a mixed regime and the filling of the lattice proceeds
according to two different processes. In the first stage, the monomers adsorb
isotropically on the lattice until the IN transition occurs in the system and,
from this point, particles adsorb forming chains so that the adlayer behaves as
a 1D fluid. The two adsorption processes are present in the adsorption
isotherms, and a marked singularity can be observed that separates both
regimes. Thus, the adsorption isotherms appear as sensitive quantities with
respect to the IN phase transition, allowing us (i) to reproduce the phase
diagram of the system for square lattices and (ii) to obtain an accurate
determination of the phase diagram for triangular lattices.Comment: Langmuir, 201
Search for the Higgs Boson at LHC in 3-3-1 Model
We present an analysis of production and signature of neutral Higgs boson
() on the version of the 3-3-1 model containing heavy leptons at the
Large Hadron Collider. We studied the possibility to identify it using the
respective branching ratios. Cross section are given for the collider energy,
14 TeV. Event rates and significances are discussed for two
possible values of integrated luminosity, 300 fb and 3000 fb.Comment: 17 pages 7 figures. arXiv admin note: substantial text overlap with
arXiv:1205.404
Estudios de acoplamiento molecular de nuevos análogos de quinolonas a la ADN girasa de Escherichia coli
Indexación: Scopus.Chemicals and CAS Registry Numbers:
amino acid, 65072-01-7; ciprofloxacin, 85721-33-1; DNA topoisomerase (ATP hydrolysing); gatifloxacin, 112811-59-3, 180200-66-2; levofloxacin, 100986-85-4, 138199-71-0; lomefloxacin, 98079-51-7; moxifloxacin, 151096-09-2; nalidixic acid, 389-08-2; oxolinic acid, 14698-29-4; pipemidic acid, 51940-44-4; rufloxacin, 101363-10-4; sitafloxacin, 127254-12-0, 163253-35-8Context: Bacterial resistance to antibiotics is the inevitable consequence of the use of antimicrobial agents. Thus, quinolones are an important class of antibacterials; these agents generally consist of a 1-subtituted-1,4-dihydro-4-oxopyridine-3-carboxylic acid moiety combined with an aromatic or heteroaromatic ring fused at the 5- and 6-position. Aims: To determine the binding of quinolones to DNA gyrase of Escherichia coli. Methods: An analysis was performed using an in silico approach to determine, by docking calculations and energy descriptors, the conformer of 4‐oxo‐1,4‐dihydroquinoline skeleton that forms the most stable complex with DNA gyrase of E. coli. Results: The complex shows that the pose of the quinolones coincides with the amino acid residues Asp87, Thr88, Arg91 and Met92, which is expected to be critical in the binding of quinolones to DNA gyrase of E. coli. A series of quinolones were computationally designed, and the interactions between the quinolones and the amino acid residues of the DNA gyrase were calculated. Conclusions: Among the designed compounds, compounds 105 and 115 exhibit higher binding energy values and interact with amino acids Asp87, Thr88, Arg91 and Met92. © 2018 Journal of Pharmacy & Pharmacognosy Research.http://jppres.com/jppres/pdf/vol6/jppres18.368_6.5.386.pd
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