Structural transitions in model beta-sheet tapes.
We present a molecular-scale simulation study of the structural transitions between helicoidal, helical, and tubular geometries in supramolecular beta-sheet tapes. Such geometries have been observed in different self-assembled amyloid systems (based on either natural or synthetic peptides) for which the beta-sheet tapes represent the simplest fibrillar aggregates. A coarse-grained model for the beta-sheet tapes is proposed, with chiral degrees of freedom and asymmetrical chemical properties, which provides a quantitative characterization of the structural transitions. A quantitative connection is established between the molecular properties and the elastic parameters of the supramolecular tapes.
Bellesia
Giovanni
G
School of Chemistry and Chemical Biology, University College Dublin, Belfield, Dublin 4, Ireland. gbellesia@chem.ucsb.edu
Fedorov
Maxim V
MV
Timoshenko
Edward G
EG
D001703:Biophysics / Q000379:methods; D002627:Chemistry, Physical / Q000379:methods; D008958:Models, Molecular; D015233:Models, Statistical; D008962:Models, Theoretical; D008968:Molecular Conformation; D009010:Monte Carlo Method; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
D010455:Peptides; D011506:Proteins