Anzeige
Erschienen in:
2014 | OriginalPaper | Buchkapitel
All-Atom Monte Carlo Simulations of Protein Folding and Aggregation
verfasst von : Anders Irbäck, Sandipan Mohanty
Erschienen in: Computational Methods to Study the Structure and Dynamics of Biomolecules and Biomolecular Processes
Verlag: Springer Berlin Heidelberg
Aktivieren Sie unsere intelligente Suche, um passende Fachinhalte oder Patente zu finden.
Wählen Sie Textabschnitte aus um mit Künstlicher Intelligenz passenden Patente zu finden. powered by
Markieren Sie Textabschnitte, um KI-gestützt weitere passende Inhalte zu finden. powered by
The ability to aggregate into
β
-sheet-rich fibrillar structures is a common property shared by many proteins. However, the propensity to aggregate and the precise mechanisms involved vary from protein to protein. Two currently intensely studied proteins are the Alzheimer’s-related amyloid
β
-peptide (A
β
) and the Parkinson’s-related
α
-synuclein (
α
S), both of which are disordered as free monomers and form fibrils. Here, we present studies of A
β
monomers and dimers and monomeric
α
S, based on an implicit solvent all-atom Monte Carlo (MC) approach. Somewhat unexpectedly, in the
α
S study, two distinct phases are observed. As a result, in the simulations, disordered
α
S has to overcome a rather large free-energy barrier in order to acquire a fibril-like fold. No corresponding barrier is observed in the A
β
simulations. Recently, the same computational model was used to study the folding of the Top7 protein, with > 90 residues and a mixed
α
+
β
fold. This chapter provides a summary of these A
β
,
α
S and Top7 studies.