Binding structures of SERF1a with the N-terminal fragment of huntingtin exon 1 and NT17-polyQ peptides are revealed using an integrated analysis of size-exclusion-column-based small- and wide-angle X-ray scattering (SEC-SWAXS), NMR, and molecular simulation.

An infrared free-electron laser was applied to dissociate amyloid fibrils of a peptide as a goal of the development of a novel therapeutic strategy for amyloidosis. Solid evidence for β-sheet to α-helix conversion in the peptide fibril by vibrational excitation of amide bonds was obtained by both experiment and molecular dynamics simulation.