The structure of misfolded amyloidogenic dimers: computational analysis of force spectroscopy data.

ABSTRACT: Progress in understanding the molecular mechanism of self-assembly of amyloidogenic proteins and peptides requires knowledge about their structure in misfolded states. Structural studies of amyloid aggregates formed during the early aggregation stage are very limited. Atomic force microscopy (AFM) spectroscopy is widely used to analyze misfolded proteins and peptides, but the structural characterization of transiently formed misfolded dimers is limited by the lack of computational approaches that allow direct comparison with AFM experiments. Steered molecular dynamics (SMD) simulation is capable of modeling force spectroscopy experiments, but the modeling requires pulling rates 10(7) times higher than those used in AFM experiments. In this study, we describe a computational all-atom Monte

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC4269799 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature