Ontology highlight
ABSTRACT:
SUBMITTER: Hills RD
PROVIDER: S-EPMC1997311 | biostudies-literature | 2007 May
REPOSITORIES: biostudies-literature
Hills Ronald D RD Brooks Charles L CL
Journal of molecular biology 20070224 3
The kinetics of amyloid fibril formation are in most cases explained by classical nucleation theory, yet the mechanisms behind nucleation are not well understood. We show using molecular dynamics simulations that the hydrophobic cooperativity in the self-association of the model amyloidogenic peptide STVIYE is sufficient to allow for nucleation-dependent polymerization with a pentamer critical nucleus. The role of electrostatics was also investigated. Novel considerations of the electrostatic so ...[more]