Fluorescence Resonance Energy Transfer (FRET) was used to study protein structures within soluble oligomer intermediates of amyloid and non-amyloid aggregates. Three protein aggregation systems were studied using fluorescence donor and acceptor near the N and C terminus:(1) Alzheimer's Ab 1-40 peptide.(2) 20-residue polyglutamine K 2 Q 16 K 2 .(3) 20-residue polyglutamic acid E 20 . (non-amyloid) The aggregation of each peptide showed different conformational changes: Ab 1-40 partially compacted into a structure consistent with solid-state NMR structures, K 2 Q 16 K 2 extended to form b-sheets, and E 20 compacted heavily into b-hairpins. However, based on donor-acceptor distances, soluble oligomers conformations of all three peptides show a remarkable degree of similarity to their monomeric precursors, albeit with a slightly expanded conformation for Ab 1-40 and E 20 . These findings support assembly models of small soluble oligomers which largely consist of monomer-like structures, with some increase in a-helical content for Ab 1-40 . These donor-acceptor distances are used to directly assess the accuracy of different molecular dynamics force fields in the study of these soluble oligomers.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.