Fast scintillation detectors for high-energy X-ray region

We have developed fast scintillation detectors for nuclear resonant scattering experiments using synchrotron radiation and a nuclear excited level existing in >30?keV. A fast x-ray detector using an organic-inorganic perovskite scintillator of phenethylamine lead bromide (PhE-PbBr₄) had a dominant light emission with a fast decay time of 9.9?ns. An x-ray detector equipped with a 0.9-mm-thick PhE-PbBr₄ crystal (size: ～8 × 7?mm²) was used to detect nuclear resonant scattering in ⁶¹Ni (the first excited level: 67.41?keV; half-life: 5.3?ns). We could successfully record the decaying gamma rays emitted from ⁶¹Ni with a relatively high detection efficiency of 24%. A lead-doped plastic scintillator (NE142, Pb ～5?wt% doped) had been known to have a faster decay time of 1.7?ns. Following a test of a single NE142 detector, a four-channel NE142 detector was fabricated and successfully applied to the synchrotron-radiation based M?ssbauer spectroscopy experiment on ⁶¹Ni.     

Modified Protein-Water Interactions in CHARMM36m for Thermodynamics and Kinetics of Proteins in Dilute and Crowded Solutions

Proper balance between protein-protein and protein-water interactions is vital for atomistic molecular dynamics (MD) simulations of globular proteins as well as intrinsically disordered proteins (IDPs). The overestimation of protein-protein interactions tends to make IDPs more compact than those in experiments. Likewise, multiple proteins in crowded solutions are aggregated with each other too strongly. To optimize the balance, Lennard-Jones (LJ) interactions between protein and water are often increased about 10% (with a scaling parameter, λ = 1.1) from the existing force fields. Here, we explore the optimal scaling parameter of protein-water LJ interactions for CHARMM36m in conjunction with the modified TIP3P water model, by performing enhanced sampling MD simulations of several peptides in dilute solutions and conventional MD simulations of globular proteins in dilute and crowded solutions. In our simulations, 10% increase of protein-water LJ interaction for the CHARMM36m cannot maintain stability of a small helical peptide, (AAQAA)₃ in a dilute solution and only a small modification of protein-water LJ interaction up to the 3% increase (λ = 1.03) is allowed. The modified protein-water interactions are applicable to other peptides and globular proteins in dilute solutions without changing thermodynamic properties from the original CHARMM36m. However, it has a great impact on the diffusive properties of proteins in crowded solutions, avoiding the formation of too sticky protein-protein interactions.     

Improved resolution for aerial imaging by retro-reflection with two transparent spheres

Optical Review - This paper proposes a method to improve the modulation transfer function (MTF) of aerial images by combining an aerial imaging optical system by retro-reflection with conjugated...