---
res:
  bibo_abstract:
  - The prevalence of proline residues in intrinsically disordered proteins, functional
    hinges of enzymes, and protein interaction sites highlights the importance of
    studying their local dynamics and interactions at atomic resolution. While nuclear
    magnetic resonance (NMR) spectroscopy is, in principle, ideally suited for such
    investigations, the absence of an amide proton precludes the use of conventional
    1H–15N amide-detected experiments. 1H–13C-based approaches, though possible, remain
    challenging in large proteins. In this work, we present a selective labeling strategy
    that introduces an isolated 1H2δ–13Cδ–15N spin system in proline residues in otherwise
    deuterated proteins. Our method leverages the enzymatic conversion of ornithine,
    synthesized from cost-effective isotopic precursors. We demonstrate the utility
    of this approach by applying it to a 134 kDa enzyme using magic-angle spinning
    NMR, highlighting its potential to efficiently probe functionally relevant sites
    in proteins.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Darja
      foaf_name: Rohden, Darja
      foaf_surname: Rohden
      foaf_workInfoHomepage: http://www.librecat.org/personId=81dc668a-19fa-11f0-bf31-d56534059ef3
  - foaf_Person:
      foaf_givenName: Federico
      foaf_name: Napoli, Federico
      foaf_surname: Napoli
      foaf_workInfoHomepage: http://www.librecat.org/personId=d42e08e7-f4fc-11eb-af0a-d71e26138f1b
    orcid: 0000-0002-9043-136X
  - foaf_Person:
      foaf_givenName: Roman J.
      foaf_name: Lichtenecker, Roman J.
      foaf_surname: Lichtenecker
  - foaf_Person:
      foaf_givenName: Paul
      foaf_name: Schanda, Paul
      foaf_surname: Schanda
      foaf_workInfoHomepage: http://www.librecat.org/personId=7B541462-FAF6-11E9-A490-E8DFE5697425
    orcid: 0000-0002-9350-7606
  bibo_doi: 10.1021/acschembio.6c00587
  dct_date: 2026^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/1554-8929
  - http://id.crossref.org/issn/1554-8937
  dct_language: eng
  dct_publisher: American Chemical Society@
  dct_title: Chemoenzymatic proline isotope labeling for solution and magic-angle
    spinning protein nuclear magnetic resonance@
  fabio_hasPubmedId: '42863127'
...