Intramolecular Diffusion in α-Synuclein: It Depends on How You Measure It.

ABSTRACT: Intramolecular protein diffusion, the motion of one part of the polypeptide chain relative to another part, is a fundamental aspect of protein folding and may modulate amyloidogenesis of disease-associated intrinsically disordered proteins. Much work has determined such diffusion coefficients using a variety of probes, but there has been an apparent discrepancy between measurements using long-range probes, such as fluorescence resonance energy transfer, and short-range probes, such as Trp-Cys quenching. In this work, we make both such measurements on the same protein, α-synuclein, and confirm that such discrepancy exists. Molecular dynamics simulations suggest that such differences result from a diffusion coefficient that depends on the spatial distance between probes. Diffusional estimate

SUBMITTER: Woodard J 

PROVIDER: S-EPMC6170596 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature