A simple lattice model that captures protein folding, aggregation and amyloid formation.
The ability of many proteins to convert from their functional soluble state to amyloid fibrils can be attributed to inter-molecular beta strand formation. Such amyloid formation is associated with neurodegenerative disorders like Alzheimer's and Parkinson's. Molecular modelling can play a...
Main Authors: | Sanne Abeln, Michele Vendruscolo, Christopher M Dobson, Daan Frenkel |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2014-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3893179?pdf=render |
Similar Items
-
Disordered flanks prevent peptide aggregation.
by: Sanne Abeln, et al.
Published: (2008-12-01) -
Protein fold evolution on completed genomes : distinguishing between young and old folds
by: Abeln, Sanne
Published: (2007) -
Folding and aggregation of amyloid peptides
by: Kittner, Madeleine
Published: (2011) -
Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation.
by: Anthony W Fitzpatrick, et al.
Published: (2011-10-01) -
A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates.
by: Stefan Auer, et al.
Published: (2008-11-01)