Rippled Sheets: The Early Polyglycine Days and Recent Developments in Nylons

Abstract

The rippled sheet structure is a remarkable insight due to Pauling and Corey, that supplements the pleated sheet structure of homochiral proteins introduced in 1951. Whereas the pleated sheet was immediately adopted by the scientific community, the rippled sheet has remained more confidential since it applies only to blends of poly(L-peptides) and poly(D-peptides). The present account tells the intimate but patchy relationship developed by the author with the rippled sheet. In the 1970s, twenty years after Pauling and Corey's proposal, the rippled sheet was recognized as a valid model for the sheet structure of the achiral polyglycine, polyglycine I, which helped improve the structure of Bombyx mori silk fibroin. Very recently, pleated and rippled sheets were found to account for unsolved crystal structures of a variety of nylons. These structures help to explain a mysterious high temperature “Brill transition” first reported in nylon 6–6 by Brill in 1942.