Dataset Information

AAfrag: Interpolation routines for Monte Carlo results on secondary production in proton-proton, proton-nucleus and nucleus-nucleus interactions.

ABSTRACT: We provide a compilation of predictions of the QGSJET-II-04m model for the production of secondary species (photons, neutrinos, electrons, positrons, and antinucleons) that are covering a wide range of energies of the beam particles in proton-proton, proton-nucleus, nucleus-proton, and nucleus-nucleus reactions. The current version of QGSJET-II-04m has an improved treatment of the production of secondary particles at low energies: the parameters of the hadronization procedure have been fine-tuned, based on a number of recent benchmark experimental data, notably, from the LHCf, LHCb, and NA61 experiments. Our results for the production spectra are made publicly accessible through the interpolation routines AAfrag which are described below. Besides, we comment on the impact of Feynman scaling violation and isospin symmetry effects on antinucleon production.

SUBMITTER: Kachelrieß M

PROVIDER: S-EPMC8507204 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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AAfrag: Interpolation routines for Monte Carlo results on secondary production in proton-proton, proton-nucleus and nucleus-nucleus interactions.

Kachelrieß M M Moskalenko I V IV Ostapchenko S S

Computer physics communications 20190807

We provide a compilation of predictions of the QGSJET-II-04m model for the production of secondary species (photons, neutrinos, electrons, positrons, and antinucleons) that are covering a wide range of energies of the beam particles in proton-proton, proton-nucleus, nucleus-proton, and nucleus-nucleus reactions. The current version of QGSJET-II-04m has an improved treatment of the production of secondary particles at low energies: the parameters of the hadronization procedure have been fine-tune ...[more]

PMID: 34646051

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Project description:Purpose/objectivesMonte Carlo (MC) dose calculation has appeared in primary commercial treatment-planning systems and various in-house platforms. Dual-energy computed tomography (DECT) and metal artifact reduction (MAR) techniques complement MC capabilities. However, no publications have yet reported how proton therapy centers implement these new technologies, and a national survey is required to determine the feasibility of including MC and companion techniques in cooperative group clinical trials.Materials/methodsA 9-question survey was designed to query key clinical parameters: scope of MC utilization, validation methods for heterogeneities, clinical site-specific imaging guidance, proton range uncertainties, and how implants are handled. A national survey was distributed to all 29 operational US proton therapy centers on 13 May 2019.ResultsWe received responses from 25 centers (86% participation). Commercial MC was most commonly used for primary plan optimization (16 centers) or primary dose evaluation (18 centers), while in-house MC was used more frequently for secondary dose evaluation (7 centers). Based on the survey, MC was used infrequently for gastrointestinal, genitourinary, gynecology and extremity compared with other more heterogeneous disease sites (P < .007). Although many centers had published DECT research, only 3/25 centers had implemented DECT clinically, either in the treatment-planning system or to override implant materials. Most centers (64%) treated patients with metal implants on a case-by-case basis, with a variety of methods reported. Twenty-four centers (96%) used MAR images and overrode the surrounding tissue artifacts; however, there was no consensus on how to determine metal dimension, materials density, or stopping powers.ConclusionThe use of MC for primary dose calculation and optimization was prevalent and, therefore, likely feasible for clinical trials. There was consensus to use MAR and override tissues surrounding metals but no consensus about how to use DECT and MAR for human tissues and implants. Development and standardization of these advanced technologies are strongly encouraged for vendors and clinical physicists.

Project description:We introduce here a novel Monte Carlo simulation method for studying the interactions of hydrophobic peptides with lipid membranes. Each of the peptide's amino acids is represented as two interaction sites: one corresponding to the backbone alpha-carbon and the other to the side chain, with the membrane represented as a hydrophobic profile. Peptide conformations and locations in the membrane and changes in the membrane width are sampled using the Metropolis criterion, taking into account the underlying energetics. Using this method we investigate the interactions between the hydrophobic peptide M2delta and a model membrane. The simulations show that starting from an extended conformation in the aqueous phase, the peptide first adsorbs onto the membrane surface, while acquiring an ordered helical structure. This is followed by formation of a helical-hairpin and insertion into the membrane. The observed path is in agreement with contemporary understanding of peptide insertion into biological membranes. Two stable orientations of membrane-associated M2delta were obtained: transmembrane (TM) and surface, and the value of the water-to-membrane transfer free energy of each of them is in agreement with calculations and measurements on similar cases. M2delta is most stable in the TM orientation, where it assumes a helical conformation with a tilt of 14 degrees between the helix principal axis and the membrane normal. The peptide conformation agrees well with the experimental data; average root-mean-square deviations of 2.1 A compared to nuclear magnetic resonance structures obtained in detergent micelles and supported lipid bilayers. The average orientation of the peptide in the membrane in the most stable configurations reported here, and in particular the value of the tilt angle, are in excellent agreement with the ones calculated using the continuum-solvent model and the ones observed in the nuclear magnetic resonance studies. This suggests that the method may be used to predict the three-dimensional structure of TM peptides.

Dataset Information

AAfrag: Interpolation routines for Monte Carlo results on secondary production in proton-proton, proton-nucleus and nucleus-nucleus interactions.

Publications

AAfrag: Interpolation routines for Monte Carlo results on secondary production in proton-proton, proton-nucleus and nucleus-nucleus interactions.

Similar Datasets

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