The newly exposed strand then allows a novel beta-sheet interaction to form between the TTR subunits. This interaction and another previously identified subunit association lead to a plausible model for the specific sequence of beta-strands in one of the indefinitely repeating beta-sheets of TTR ...
The effect of cooperative interactions between β-strands in enhancing β-sheet stability has been examined quantitatively by NMR using rationally designed synthetic peptides [β-hairpin (2β) and related 24-residue three-stranded antiparallel β-sheet (3β)] which are significantly folded in aqueous...