Extended Data Fig. 5: Plot showing persistence length versus mass per unit length for various 1D polymers and molecular assemblies.

The plot is adapted with permission from ref. ¹⁶, Springer Nature Limited. For peptide-bundlemer rigid rods, the persistence length was estimated from our cryoTEM data using the methods of ref. ²¹. Other persistence lengths were taken from the following references: hydrocarbon polymers, ref. ¹⁶; fd and M13 viruses, refs. ^11,12; DNA, refs. ^16,24; actin, refs. ^13,38; tobacco mosaic virus, refs. ^16,39,40; microtubulin, refs. ^13,39,40; thin (diameter 2–3 nm) and thick (diameter 4–6 nm) twisted bovine serum albumin (BSA) fibres, ref. ²⁰; β-lactoglobulin β-sheet-rich twisted fibrils (with diameters ranging from 1 nm to 6 nm, with a mean of roughly 3 nm), ref. ^11,22; amino acid β-sheet ribbons with low stacking (producing ribbon diameters of roughly 4 nm) and high stacking (producing ribbons with diameters of 4–8 nm), ref. ²³.