Structural context modulates the conformational ensemble of the intrinsically disordered amino terminus of α-synuclein.

ABSTRACT: Regions of intrinsic disorder play crucial roles in biological systems, yet they often elude characterization by conventional biophysical techniques. To capture conformational distributions across different timescales, we employed a freezing approach coupled with solid-state NMR analysis. Using segmentally isotopically labeled α-synuclein (α-syn), we investigated the conformational preferences of the six alanines, three glycines, and a single site (L8) in the disordered amino terminus under three distinct conditions: in 8 M urea, as a frozen monomer in buffer, and within the disordered regions flanking the amyloid core. The experimental spectra varied significantly among these conditions and deviated from those of a statistical coil. In 8 M urea, monomeric α-syn exhibited the most restrict

SUBMITTER: Dumarieh R 

PROVIDER: S-EPMC11565972 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature