A lowly populated, transient β-sheet structure in monomeric Aβ^1-42 identified by multinuclear NMR of chemical denaturation.

ABSTRACT: Chemical denaturation is a well-established approach for probing the equilibrium between folded and unfolded states of proteins. We demonstrate applicability of this method to the detection of a small population of a transiently folded structural element in a system that is often considered to be intrinsically fully disordered. The ¹H^N, ¹⁵N, ¹³C^α, and ¹³C' chemical shifts of Aβ^1-40 and Aβ^1-42 peptides and their M35-oxidized variants were monitored as a function of urea concentration and compared to analogous urea titrations of synthetic pentapeptides of homologous sequence. Fitting of the chemical shift titrations yields a 10 ± 1% population for a structured element at the C-terminus of Aβ^1-42

SUBMITTER: Kakeshpour T 

PROVIDER: S-EPMC7878406 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature