Measuring the Energy Barrier of the Structural Change That Initiates Amyloid Formation.

ABSTRACT: Obtaining kinetic and thermodynamic information for protein amyloid formation can yield new insight into the mechanistic details of this biomedically important process. The kinetics of the structural change that initiates the amyloid pathway, however, has been challenging to access for any amyloid protein system. Here, using the protein β-2-microglobulin (β2m) as a model, we measure the kinetics and energy barrier associated with an initial amyloidogenic structural change. Using covalent labeling and mass spectrometry, we measure the decrease in solvent accessibility of one of β2m's Trp residues, which is buried during the initial structural change, as a way to probe the kinetics of this structural change at different temperatures and under different amyloid forming conditions. Our results

SUBMITTER: Arden BG 

PROVIDER: S-EPMC7206453 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature