Ontology highlight
ABSTRACT:
SUBMITTER: Wetzel R
PROVIDER: S-EPMC2526019 | biostudies-literature | 2007 Jan
REPOSITORIES: biostudies-literature
Wetzel Ronald R Shivaprasad Shankaramma S Williams Angela D AD
Biochemistry 20070101 1
In experiments designed to characterize the basis of amyloid fibril stability through mutational analysis of the Abeta (1-40) molecule, fibrils exhibit consistent, significant structural malleability. In these results, and in other properties, amyloid fibrils appear to more resemble plastic materials generated from synthetic polymers than globular proteins. Thus, like synthetic polymers and plastics, amyloid fibrils exhibit both polymorphism, the ability of one polypeptide to form aggregates of ...[more]