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Various models to describe small-angle neutron scattering data from helices of amyloid protofilaments (hen egg white lysozyme) in solution were analyzed. The found parameters were compared with those obtained by atomic force microscopy of the dried adsorbed state of amyloid fibrils.

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The method of classical molecular dynamics simulation is used for modeling the experimental small-angle neutron scattering from saturated monocarboxylic acids with short chain lengths in deuterated decalin solutions. It is shown that a specific organization of the solvent molecules in the solute-solvent interface area has a significant effect on the scattering.
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