32 research outputs found
Challenging SO(10) SUSY GUTs with family symmetries through FCNC processes
We perform a detailed analysis of the SO(10) SUSY GUT model with D3 family
symmetry of Dermisek and Raby (DR). The model is specified in terms of 24
parameters and predicts, as a function of them, the whole MSSM set of
parameters at low energy scales. Concerning the SM subset of such parameters,
the model is able to give a satisfactory description of the quark and lepton
masses, of the PMNS matrix and of the CKM matrix. We perform a global fit to
the model, including flavour changing neutral current (FCNC) processes Bs -->
mu+ mu-, B --> Xs gamma, B --> Xs l+ l- and the B(d,s) - bar B(d,s) mass
differences Delta M(d,s) as well as the flavour changing (FC) process B+ -->
tau+ nu. These observables provide at present the most sensitive probe of the
SUSY mass spectrum and couplings predicted by the model. Our analysis
demonstrates that the simultaneous description of the FC observables in
question represents a serious challenge for the DR model, unless the masses of
the scalars are moved to regions which are problematic from the point of view
of naturalness and probably beyond the reach of the LHC. We emphasize that this
problem could be a general feature of SUSY GUT models with third generation
Yukawa unification and weak-scale minimal flavour violation.Comment: 1 + 37 pages, 5 figures, 11 tables. v3: minor typos fixed. Matches
JHEP published versio
Nonlinearity of Mechanochemical Motions in Motor Proteins
The assumption of linear response of protein molecules to thermal noise or
structural perturbations, such as ligand binding or detachment, is broadly used
in the studies of protein dynamics. Conformational motions in proteins are
traditionally analyzed in terms of normal modes and experimental data on
thermal fluctuations in such macromolecules is also usually interpreted in
terms of the excitation of normal modes. We have chosen two important protein
motors - myosin V and kinesin KIF1A - and performed numerical investigations of
their conformational relaxation properties within the coarse-grained elastic
network approximation. We have found that the linearity assumption is deficient
for ligand-induced conformational motions and can even be violated for
characteristic thermal fluctuations. The deficiency is particularly pronounced
in KIF1A where the normal mode description fails completely in describing
functional mechanochemical motions. These results indicate that important
assumptions of the theory of protein dynamics may need to be reconsidered.
Neither a single normal mode, nor a superposition of such modes yield an
approximation of strongly nonlinear dynamics.Comment: 10 pages, 6 figure
Glycine insertion makes yellow fluorescent protein sensitive to hydrostatic pressure
Fluorescent protein-based indicators for intracellular environment conditions such as pH and ion concentrations are commonly used to study the status and dynamics of living cells. Despite being an important factor in many biological processes, the development of an indicator for the physicochemical state of water, such as pressure, viscosity and temperature, however, has been neglected. We here found a novel mutation that dramatically enhances the pressure dependency of the yellow fluorescent protein (YFP) by inserting several glycines into it. The crystal structure of the mutant showed that the tyrosine near the chromophore flipped toward the outside of the β-can structure, resulting in the entry of a few water molecules near the chromophore. In response to changes in hydrostatic pressure, a spectrum shift and an intensity change of the fluorescence were observed. By measuring the fluorescence of the YFP mutant, we succeeded in measuring the intracellular pressure change in living cell. This study shows a new strategy of design to engineer fluorescent protein indicators to sense hydrostatic pressure
Acetyl-11-keto-β-boswellic acid (AKBA); targeting oral cavity pathogens
<p>Abstract</p> <p>Background</p> <p>Boswellic acids mixture of triterpenic acids obtained from the oleo gum resin of <it>Boswellia serrata </it>and known for its effectiveness in the treatment of chronic inflammatory disease including peritumor edema. Boswellic acids have been extensively studied for a number of activities including anti inflammatory, antitumor, immunomodulatory, and inflammatory bowel diseases. The present study describes the antimicrobial activities of boswellic acid molecules against oral cavity pathogens. Acetyl-11-keto-β-boswellic acid (AKBA), which exhibited the most potent antibacterial activity, was further evaluated in time kill studies, mutation prevention frequency, postantibiotic effect (PAE) and biofilm susceptibility assay against oral cavity pathogens.</p> <p>Findings</p> <p>AKBA exhibited an inhibitory effect on all the oral cavity pathogens tested (MIC of 2-4 μg/ml). It exhibited concentration dependent killing of S<it>treptococcus mutans </it>ATCC 25175 up to 8 × MIC and also prevented the emergence of mutants of <it>S.mutans </it>ATCC 25175 at 8× MIC. AKBA demonstrated postantibiotic effect (PAE) of 5.7 ± 0.1 h at 2 × MIC. Furthermore, AKBA inhibited the formation of biofilms generated by <it>S.mutans </it>and <it>Actinomyces viscosus </it>and also reduced the preformed biofilms by these bacteria.</p> <p>Conclusions</p> <p>AKBA can be useful compound for the development of antibacterial agent against oral pathogens and it has great potential for use in mouthwash for preventing and treating oral infections.</p