Analytical Methods for Analysis of Neutron Crosssections of Amino Acids and Proteins

Voi, Dante Luiz; Ferreira, Francisco de O.; Rocha, Hélio Fernandes da; Nunes, Rogério Chaffin; Carvalheira, Luciana

doi:10.29327/146852.8-1

Cited by 2 publications

(2 citation statements)

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“…Following the 1/ω dependence in equation ( 6), one can expect that a slight error in the calculation of the intensities of g i (ω → 0) becomes particularly evident on the final result, and especially at higher values of T. It is also important to note that the calculation of σ(E) using m2, i.e., applying the MPE only to hydrogen and using σ f,i for the other elements, provides a significantly simpler approach and substantially lower computational costs, yet obtaining a very accurate result. Experimental results for the neutron cross section of amino acids were previously presented in reference [90] at one value of the incident neutron energy of 50 meV. We note that those results generally underestimate the results from the present investigation, possibly because of the uncertainties on the density and thickness of the powder samples avoided in our normalization procedure [31].…”

Section: Resultscontrasting

confidence: 67%

Thermal neutron cross sections of amino acids from average contributions of functional groups

Romanelli

Onorati

Ulpiani

et al. 2021

J. Phys.: Condens. Matter

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The experimental thermal neutron cross sections of the 20 proteinogenic amino acids have been measured over the incident-neutron energy range spanning from 1 meV to 10 keV and data have been interpreted using the multi-phonon expansion based on first-principles calculations. The scattering cross section, dominated by the incoherent inelastic contribution from the hydrogen atoms, can be rationalised in terms of the average contributions of different functional groups, thus neglecting their correlation. These results can be used for modelling the total neutron cross sections of complex organic systems like proteins, muscles, or human tissues from a limited number of starting input functions. This simplification is of crucial importance for fine-tuning of transport simulations used in medical applications, including boron neutron capture therapy as well as secondary neutrons-emission induced during proton therapy. Moreover, the parametrized neutron cross sections allow a better treatment of neutron scattering experiments, providing detailed sample self-attenuation corrections for a variety of biological and soft-matter systems.

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Section: Resultscontrasting

confidence: 67%

Thermal neutron cross sections of amino acids from average contributions of functional groups

Romanelli

Onorati

Ulpiani

et al. 2021

J. Phys.: Condens. Matter

View full text Add to dashboard Cite

show abstract

“…Experimental results for the neutron cross section of amino acids were previously pre- sented in Ref. 89 at one value of the incident neutron energy of 50 meV. We note that those results generally underestimate the results from the present investigation, possibly because of the uncertainties on the density and thickness of the powder samples avoided in our normalization procedure 29 .…”

Section: Resultscontrasting

confidence: 62%

Thermal neutron cross sections of amino acids from average contributions of functional groups

Romanelli,

Onorati,

Ulpiani

et al. 2021

Preprint

View full text Add to dashboard Cite

The experimental thermal neutron cross sections of the twenty proteinogenic amino acids have been measured over the incident-neutron energy range spanning from 1 meV to 10 keV and data have been interpreted using the multi-phonon expansion based on first-principles calculations. The scattering cross section, dominated by the incoherent inelastic contribution from the hydrogen atoms, can be rationalised in terms of the average contributions of different functional groups, thus neglecting their correlation. These results can be used for modelling the total neutron cross sections of complex organic systems like proteins, muscles, or human tissues from a limited number of starting input functions. This simplification is of crucial importance for fine-tuning of transport simulations used in medical applications, including boron neutron capture therapy as well as secondary neutrons-emission induced during proton therapy. Moreover, the parametrized neutron cross sections allow a better treatment of neutron scattering experiments, providing detailed sample self-attenuation corrections for a variety of biological and soft-matter systems.

show abstract

Analytical Methods for Analysis of Neutron Crosssections of Amino Acids and Proteins

Cited by 2 publications

References 1 publication

Thermal neutron cross sections of amino acids from average contributions of functional groups

Thermal neutron cross sections of amino acids from average contributions of functional groups

Thermal neutron cross sections of amino acids from average contributions of functional groups

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