Skip to main content
. Author manuscript; available in PMC: 2019 May 31.
Published in final edited form as: J Phys Chem B. 2018 Mar 9;122(21):5567–5578. doi: 10.1021/acs.jpcb.7b11830

Figure 1.

Figure 1

High resolution structures of amyloid fibrils show β-sheets composed of molecules perfectly aligned in the in-register state (left). However, fibrils grown at very high concentrations or grown from molecules with poor templating specificity can contain alignment defects (right). We describe the alignment between an incoming molecule (grey) and the existing fibril (black) using the registry variable R.