Ontology highlight
ABSTRACT:
SUBMITTER: Fandrich M
PROVIDER: S-EPMC307590 | biostudies-literature | 2003 Dec
REPOSITORIES: biostudies-literature
Fändrich Marcus M Forge Vincent V Buder Katrin K Kittler Marlis M Dobson Christopher M CM Diekmann Stephan S
Proceedings of the National Academy of Sciences of the United States of America 20031209 26
Observations that beta-sheet proteins form amyloid fibrils under at least partially denaturing conditions has raised questions as to whether these fibrils assemble by docking of preformed beta-structure or by association of unfolded polypeptide segments. By using alpha-helical protein apomyoglobin, we show that the ease of fibril assembly correlates with the extent of denaturation. By contrast, monomeric beta-sheet intermediates could not be observed under the conditions of fibril formation. The ...[more]