Side Chain Geometry Determines the Fibrillation Propensity of a Minimal Two-Beads-per-Residue Peptide Model
Author:
Affiliation:
1. Faculty of Chemistry, Adam Mickiewicz University in Poznań, Uniwersytetu Poznańskiego 8, 61-614 Poznań, Poland
Funder
European Social Fund
Uniwersytet im. Adama Mickiewicza w Poznaniu
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.2c03502
Reference40 articles.
1. Half a century of amyloids: past, present and future
2. Amyloid Fibrils: Versatile Biomaterials for Cell Adhesion and Tissue Engineering Applications
3. Protein Dynamics Simulations Using Coarse-Grained Models
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5. From amorphous aggregates to polymer bundles: The role of stiffness on structural phases in polymer aggregation
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