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Using a combination of explicit solvent atomistic simulation and continuum theory, here we study the lateral deformation mechanics of three distinct protein structures: an amyloid fibril, a beta helix, and an alpha helix. We find that the two b-sheet rich structures -amyloid fibril and beta helix, with persistence lengths on the order of mm -are well described by continuum mechanical theory, but differ in the degree to which shear deformation affects the overall bending behavior. The alphadoi:10.1039/c1nr11260k pmid:22193831 fatcat:ct4slqtomzchxf6547jktyacly