Design and first measurements of the fast-ion D-alpha diagnostic at the HL-2A tokamak.

The fast-ion D-alpha diagnostic (FIDA) is employed to detect Dα light emitted by neutralized fast ions during neutral beam injection. A tangentially viewing FIDA has been developed for the HuanLiuqi-2A (HL-2A) tokamak and typically achieves temporal and transverse spatial resolutions of ∼30 ms and ∼5 cm, respectively. A fast-ion tail on the red shifted wing of the FIDA spectrum is obtained and analyzed with the Monte Carlo code FIDASIM. Good agreement has been presented between the measured and simulated spectra. As the FIDA diagnostic's lines of sight intersect the central axis of neutral beam injection with small angles, the beam emission spectrum is observed with a large Doppler shift. Thus, tangentially viewing FIDA could detect only a small portion of fast ions with an energy of ≈ 20 ∼ 31 keV and a pitch angle of ≈ -1 ∼ -0.8. A second FIDA installation with oblique viewing is designed to minimize spectral contaminants.

Simulations of neutral beam injection and ion cyclotron resonance heating synergy in high power EAST scenarios.

The EAST plasmas heated with deuterium neutral beam injection and ion cyclotron resonance heating (ICRH) have been simulated by the TRANSP code. The analysis has been conducted using the full wave solver TORIC5, the radio frequency (RF)-kick operator, and NUBEAM to model the RF heating effects on fast ion velocity distribution. In this work, we present several simulated results compared with experiments for high power EAST scenarios, indicating that the interactions between ICRH and fast ions can significantly accelerate fast ions, which are confirmed by the increased neutron yield and broadened neutron emission spectrum measurements.

Geometric and statistical properties of the mean-field hydrophobic-polar model, the large-small model, and real protein sequences.

Lattice models, for their coarse-grained nature, are best suited for the study of the "designability problem," the phenomenon in which most of the about 16 000 proteins of known structure have their native conformations concentrated in a relatively small number of about 500 topological classes of conformations. Here it is shown that on a lattice the most highly designable simulated protein structures are those that have the largest number of surface-core switchbacks. A combination of physical, mathematical, and biological reasons that causes the phenomenon is given. By comparing the most foldable model peptides with protein sequences in the Protein Data Bank, it is shown that whereas different models may yield similar designabilities, predicted foldable peptides will simulate natural proteins only when the model incorporates the correct physics and biology, in this case if the main folding force arises from the differing hydrophobicity of the residues, but does not originate, say, from the steric hindrance effect caused by the differing sizes of the residues.

Mean-field HP model, designability and alpha-helices in protein structures.

Analysis of the geometric properties of a mean-field HP model on a square lattice for protein structure shows that structures with a large number of switchbacks between surface and core sites are chosen favorably by peptides as unique ground states. Global comparison of model (binary) peptide sequences with concatenated (binary) protein sequences listed in the Protein Data Bank and the Dali Domain Dictionary indicates that the highest correlation occurs between model peptides choosing the favored structures and those portions of protein sequences containing alpha helices.