ArticleJournal of the American Chemical Society2024
Enhancing Sensitivity of Nuclear Magnetic Resonance in Biomolecules: Parahydrogen-Induced Hyperpolarization in Synthetic Disulfide-Rich Miniproteins.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Hyperpolarization of small peptides by parahydrogen-induced polarization (PHIP) to increase the sensitivity of nuclear magnetic resonance (NMR) techniques is well established, while its application to larger biopolymers is still a mainly unexplored area. A particular challenge is the presence of folding-essential disulfide bridges. They tend to form metal complexes, thus hampering catalytic hydrogenation, a prerequisite for PHIP. We applied the PHIP technique to enhance NMR signal intensity in cystine-knot miniproteins─highly ordered peptide architectures covalently stabilized by three disulfides. To achieve PHIP, we introduced an l-propargyl tyrosine label at different positions in three synthetic open-chain variants of a natural trypsin inhibitor MCoTI-II. For the folded cystine knot, we observed NMR signal enhancements of up to 499 in methanol, 307 in a D
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