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The experimental thermal neutron cross sections of the twenty proteinogenicamino acids have been measured over the incident-neutron energy range spanningfrom 1 meV to 10 keV and data have been interpreted using the multi-phononexpansion based on first-principles calculations. The scattering cross section,dominated by the incoherent inelastic contribution from the hydrogen atoms, canbe rationalised in terms of the average contributions of different functionalgroups, thus neglecting their correlation. These results can be used formodelling the total neutron cross sections of complex organic systems likeproteins, muscles, or human tissues from a limited number of starting inputfunctions. This simplification is of crucial importance for fine-tuning oftransport simulations used in medical applications, including boron neutroncapture therapy as well as secondary neutrons-emission induced during protontherapy. Moreover, the parametrized neutron cross sections allow a bettertreatment of neutron scattering experiments, providing detailed sampleself-attenuation corrections for a variety of biological and soft-mattersystems.

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