130 research outputs found
A search for new particles in proton‐nucleus collisions at 400 GeV/c
We report preliminary results from a search for new particles produced in proton‐nucleus collisions at 400 GeV/c. A double‐arm spectrometer is used to detect two‐body final states where each spectrometer arm has the capability of uniquely identifying Π±, K±, p, ?, μ±, and ϕ. The Jψ is measured in the μ+μ− mode.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/87398/2/30_1.pd
Spin observables of the reactions NN -> DeltaN and pd -> Delta (pp)(1S0) in collinear kinematics
A general formalism for double and triple spin-correlations of the reaction
NN -> DeltaN is developed for the case of collinear kinematics. A complete
polarization experiment allowing to reconstruct all of the four amplitudes
describing this process is suggested. Furthermore, the spin observables of the
inelastic charge-exchange reaction pd -> Delta^0(pp)(1S0) are analyzed in
collinear kinematics within the single pN scattering mechanism involving the
subprocess pn -> Delta^0p. The full set of spin observables related to the
polarization of one or two initial particles and one final particle is obtained
in terms of three invariant amplitudes of the reaction pd -> Delta (pp)(1S0)
and the transition form factor d->(pp)(1S0). A complete polarization experiment
for the reaction pd -> Delta^0(pp)(1S0) is suggested which allows one to
determine three independent combinations of the four amplitudes of the
elementary subprocess NN -> DeltaN.Comment: 12 pages, 1 figur
An updated analysis of NN elastic scattering data to 1.6 GeV
An energy-dependent and set of single-energy partial-wave analyses of
elastic scattering data have been completed. The fit to 1.6~GeV has been
supplemented with a low-energy analysis to 400 MeV. Using the low-energy fit,
we study the sensitivity of our analysis to the choice of coupling
constant. We also comment on the possibility of fitting data alone. These
results are compared with those found in the recent Nijmegen analyses. (Figures
may be obtained from the authors upon request.)Comment: 17 pages of text, VPI-CAPS-7/
New limits on D0 (1.865) production in proton-nucleus collisions at 400 GeV/c
We present final results of a sensitive search for new particles in [pi]+/-K[mnplus] effective mass spectra observed in proton-nucleus collisions at 400 GeV/c. We establish a limit for D0 (1.865) production B[pi]+[pi]- d[sigma]/dy ycm[approximate] -0.4. For D0 --> [pi]-K+ the limit is 290 nb/nucleon.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/22811/1/0000369.pd
Molecular Dynamics and Quantum Mechanics of RNA: Conformational and Chemical Change We Can Believe In
Structure and dynamics are both critical to RNA’s vital functions in biology. Numerous techniques can elucidate the structural dynamics of RNA, but computational approaches based on experimental data arguably hold the promise of providing the most detail. In this Account, we highlight areas wherein molecular dynamics (MD) and quantum mechanical (QM) techniques are applied to RNA, particularly in relation to complementary experimental studies
Revision of AMBER Torsional Parameters for RNA Improves Free Energy Predictions for Tetramer Duplexes with GC and iGiC Base Pairs
All-atom force fields are important for predicting thermodynamic, structural, and dynamic properties of RNA. In this paper, results are reported for thermodynamic integration calculations of free energy differences of duplex formation when CG pairs in the RNA duplexes r(CCGG)2, r(GGCC)2, r(GCGC)2, and r(CGCG)2 are replaced by isocytidine–isoguanosine (iCiG) pairs. Agreement with experiment was improved when ε/ζ, α/γ, β, and χ torsional parameters in the AMBER99 force field were revised on the basis of quantum mechanical calculations. The revised force field, AMBER99TOR, brings free energy difference predictions to within 1.3, 1.4, 2.3, and 2.6 kcal/mol at 300 K, respectively, compared to experimental results for the thermodynamic cycles of CCGG → iCiCiGiG, GGCC → iGiGiCiC, GCGC → iGiCiGiC, and CGCG → iCiGiCiG. In contrast, unmodified AMBER99 predictions for GGCC → iGiGiCiC and GCGC → iGiCiGiC differ from experiment by 11.7 and 12.6 kcal/mol, respectively. In order to test the dynamic stability of the above duplexes with AMBER99TOR, four individual 50 ns molecular dynamics (MD) simulations in explicit solvent were run. All except r(CCGG)2 retained A-form conformation for ≥82% of the time. This is consistent with NMR spectra of r(iGiGiCiC)2, which reveal an A-form conformation. In MD simulations, r(CCGG)2 retained A-form conformation 52% of the time, suggesting that its terminal base pairs may fray. The results indicate that revised backbone parameters improve predictions of RNA properties and that comparisons to measured sequence dependent thermodynamics provide useful benchmarks for testing force fields and computational methods
Understanding the Origins of Bacterial Resistance to Aminoglycosides through Molecular Dynamics Mutational Study of the Ribosomal A-Site
Paromomycin is an aminoglycosidic antibiotic that targets the RNA of the bacterial small ribosomal subunit. It binds in the A-site, which is one of the three tRNA binding sites, and affects translational fidelity by stabilizing two adenines (A1492 and A1493) in the flipped-out state. Experiments have shown that various mutations in the A-site result in bacterial resistance to aminoglycosides. In this study, we performed multiple molecular dynamics simulations of the mutated A-site RNA fragment in explicit solvent to analyze changes in the physicochemical features of the A-site that were introduced by substitutions of specific bases. The simulations were conducted for free RNA and in complex with paromomycin. We found that the specific mutations affect the shape and dynamics of the binding cleft as well as significantly alter its electrostatic properties. The most pronounced changes were observed in the U1406C∶U1495A mutant, where important hydrogen bonds between the RNA and paromomycin were disrupted. The present study aims to clarify the underlying physicochemical mechanisms of bacterial resistance to aminoglycosides due to target mutations
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