Charge Regulation during Amyloid Formation of α-Synuclein.

ABSTRACT: Electrostatic interactions play crucial roles in protein function. Measuring pK_a value perturbations upon complex formation or self-assembly of e.g. amyloid fibrils gives valuable information about the effect of electrostatic interactions in those processes. Site-specific pK_a value determination by solution NMR spectroscopy is challenged by the high molecular weight of amyloid fibrils. Here we report a pH increase during fibril formation of α-synuclein, observed using three complementary experimental methods: pH electrode measurements in water; colorimetric changes of a fluorescent indicator; and chemical shift changes for histidine residues using solution state NMR spectroscopy. A significant pH increase was detected during fibril formation in water, on

SUBMITTER: Palmadottir T 

PROVIDER: S-EPMC8161422 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature