The Inside Back Cover summarizes the strategy applied to study the influence of local physical forces on the fibrillation kinetics, structure, and dynamics of amyloid β (1–40) fibrils. Rationally designed mutations were introduced to modify the hydrophobic contact between residues 19 and 34. More information can be found in the Full Paper by J. Adler et al. on
page 2744 in Issue 17, 2016 (DOI:
10.1002/cphc.201600413).