... acidicconditions are unlikely to alter the conformation signi®-cantly. The backscattered Raman and R OA spectra of the wild-type and mutant tau46 are shown as the top and bottom pairs, respectively, ... onformational elementsare similar and hence that the structures of the caseins,synucleins and tau may be envisaged as more open,hydrated, longer-chain (and nonglobular) versions of the structure of ... structure,possibly b ased on the PPII conformation, and which may b eenvisaged as a more open version of the X -ray crystalstructure of the Bowman±Birk inhibitor. The rheomorphiccharacter i mparted by large...