<i>In Cellulo</i> Cysteine Umpolung for Protein Structure Probing.

ABSTRACT: Proteome-wide intramolecular cross-linking of amino acids allows for protein structure probing and is often achieved by reactive intermediates generated in situ. For example, carbene insertion chemistry forms versatile products but relies on two-step protocols that first introduce a photoreactive group and then generate a reactive intermediate via UV light irradiation. Alternatively, direct cross-linking with bifunctional electrophilic reagents enables modification of natural amino acids in a single transformation but proceeds via intermediates with a sufficiently long half-life in solution to capture unfavorable protein conformations. Herein, we report the use of commercially available vinyl thianthrenium tetrafluoroborate (VTT) for a single-step cross-linking strategy based

SUBMITTER: Hartmann P 

PROVIDER: S-EPMC12498408 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature