Fenton-Chemistry-Based Oxidative Modification of Proteins Reflects Their Conformation.

ABSTRACT: In order to understand protein structure to a sufficient extent for, e.g., drug discovery, no single technique can provide satisfactory information on both the lowest-energy conformation and on dynamic changes over time (the 'four-dimensional' protein structure). Instead, a combination of complementary techniques is required. Mass spectrometry methods have shown promise in addressing protein dynamics, but often rely on the use of high-end commercial or custom instruments. Here, we apply well-established chemistry to conformation-sensitive oxidative protein labelling on a timescale of a few seconds, followed by analysis through a routine protein analysis workflow. For a set of model proteins, we show that site selectivity of labelling can indeed be rationalised in terms of known structural

SUBMITTER: Nehls T 

PROVIDER: S-EPMC8469487 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature