ArticleJournal of the American Chemical Society2025
Isoleucine Side Chains as Reporters of Conformational Freedom in Protein Folding Studied by DNP-Enhanced NMR.
Leonardo Levorin, Nina Becker, Boran Uluca-Yazgi, Luis Gardon, Mirko Kraus, Marc Sevenich, Athina Apostolidis, Kai Schmitz, Neomi Rüter, Irina Apanasenko and 5 more
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In one paragraphArticle in Journal of the American Chemical Society, 2025. 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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5 · Who and what moneyAuthors and funding
15 authors.
Leonardo LevorinInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.ORCID 0009-0006-5814-4367 Nina BeckerInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.
Boran Uluca-YazgiInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.
Luis GardonInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.ORCID 0000-0003-0871-6487 Mirko KrausInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.
Marc SevenichInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.
Athina ApostolidisInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.
Kai SchmitzInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.
Neomi RüterInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.
Irina ApanasenkoInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.
Dieter WillboldInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.ORCID 0000-0002-0065-7366 Wolfgang HoyerInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.
Philipp NeudeckerInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.ORCID 0000-0002-0557-966X Lothar GremerInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.ORCID 0000-0001-7065-5027 Henrike HeiseInstitute of Physical Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf 40225, Germany.ORCID 0000-0002-9081-3894 Funding
No grant is acknowledged in the PubMed record.
6 · The paper itselfAbstract
Conformations of protein side chains are closely linked to protein function. DNP-enhanced solid-state NMR (ssNMR), which operates at cryogenic temperatures (<110 K), can be used to freeze-trap protein conformations, including the side chains. In the present study, we employed two-dimensional DNP-enhanced ssNMR to get detailed insights into backbone and side chain conformations of isoleucine. We used different amino acid selectively labeled model proteins for intrinsically disordered proteins (IDPs), denatured and well-folded proteins, and amyloid fibrils.
Indexed as
IsoleucineNuclear Magnetic Resonance, BiomolecularAnimalsCattleIntrinsically Disordered ProteinsPhosphatidylinositol 3-KinasesProtein ConformationProtein Foldingsrc Homology DomainsIntrinsically Disordered ProteinsIsoleucinePhosphatidylinositol 3-Kinases
Identifiers
PMID40285725
PMCPMC12063180
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