Comparing an intrinsically disordered protein α-synuclein to fixed structure proteins following FPOP modification using high resolution LCMS intact analysis

DPs are typically defined as lacking a fixed structure however there is growing evidence that IDPs play an important role in cell signalling and various pathological states. Misfolding and aggregation of α-synuclein form a major component in Lewy bodies which form the main pathogenesis of Parkinson’s disease (PD) and thus characterisation of differing conformational states of IDPs is vital to the understanding of disorders such as PD. In this work a technique known as FPOP was used to oxidatively modify several model proteins in order to compare modification efficiency of fixed conformation proteins verses the IDP α-synuclein.