Burst Phase Analysis of the Aggregation Prone α-synuclein Amyloid Protein.

ABSTRACT: While some studies inferred that valid information can be retrieved for the refolding of proteins and consequent identification of folding intermediates in the stopped-flow spectrometry collapse phase, other studies report that these burst phase folding intermediates can be questioned, implying a solvent-dependent modification of the still unfolded polypeptide chain. We therefore decided to investigate the burst phase occurring for the α-synuclein (Syn) amyloid protein by stopped-flow spectrometry. Solvent-dependent modification effects indeed occurred for the N_α-acetyl-L-tyrosinamide (NAYA) parent small compound and for the folded monomeric ubiquitin protein. More complex was the burst phase analysis of the disordered Syn amyloid protein. While this amyloid protein was determin

SUBMITTER: Saraiva MA 

PROVIDER: S-EPMC10808200 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature