---
OA_place: publisher
OA_type: hybrid
_id: '23173'
abstract:
- lang: eng
  text: 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.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: We thank Undina Guillerm, Rajkumar Singh and Anna Kapitonova for
  help with protein production. We are grateful to Dominique Madern for discussions
  and for providing the plasmid of IiMDH. We acknowledge the Scientific Service Units
  (SSU) of the Institute of Science and Technology Austria (ISTA) through resources
  provided by the NMR Facility and the Lab Support Facility, as well as the NMR centre
  and MS centre of the University of Vienna. This work was supported by the Austrian
  Science Fund (FWF; project number I5812-B) through a French-Austrian binational
  research project, as well as by the L’Oréal-UNESCO For Women in Science Fellowship,
  awarded in cooperation with the Austrian Academy of Sciences (ÖAW) and the Austrian
  Commission for UNESCO.
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Darja
  full_name: Rohden, Darja
  id: 81dc668a-19fa-11f0-bf31-d56534059ef3
  last_name: Rohden
- first_name: Federico
  full_name: Napoli, Federico
  id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
  last_name: Napoli
  orcid: 0000-0002-9043-136X
- first_name: Roman J.
  full_name: Lichtenecker, Roman J.
  last_name: Lichtenecker
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Rohden D, Napoli F, Lichtenecker RJ, Schanda P. Chemoenzymatic proline isotope
    labeling for solution and magic-angle spinning protein nuclear magnetic resonance.
    <i>ACS Chemical Biology</i>. 2026. doi:<a href="https://doi.org/10.1021/acschembio.6c00587">10.1021/acschembio.6c00587</a>
  apa: Rohden, D., Napoli, F., Lichtenecker, R. J., &#38; Schanda, P. (2026). Chemoenzymatic
    proline isotope labeling for solution and magic-angle spinning protein nuclear
    magnetic resonance. <i>ACS Chemical Biology</i>. American Chemical Society. <a
    href="https://doi.org/10.1021/acschembio.6c00587">https://doi.org/10.1021/acschembio.6c00587</a>
  chicago: Rohden, Darja, Federico Napoli, Roman J. Lichtenecker, and Paul Schanda.
    “Chemoenzymatic Proline Isotope Labeling for Solution and Magic-Angle Spinning
    Protein Nuclear Magnetic Resonance.” <i>ACS Chemical Biology</i>. American Chemical
    Society, 2026. <a href="https://doi.org/10.1021/acschembio.6c00587">https://doi.org/10.1021/acschembio.6c00587</a>.
  ieee: D. Rohden, F. Napoli, R. J. Lichtenecker, and P. Schanda, “Chemoenzymatic
    proline isotope labeling for solution and magic-angle spinning protein nuclear
    magnetic resonance,” <i>ACS Chemical Biology</i>. American Chemical Society, 2026.
  ista: Rohden D, Napoli F, Lichtenecker RJ, Schanda P. 2026. Chemoenzymatic proline
    isotope labeling for solution and magic-angle spinning protein nuclear magnetic
    resonance. ACS Chemical Biology.
  mla: Rohden, Darja, et al. “Chemoenzymatic Proline Isotope Labeling for Solution
    and Magic-Angle Spinning Protein Nuclear Magnetic Resonance.” <i>ACS Chemical
    Biology</i>, American Chemical Society, 2026, doi:<a href="https://doi.org/10.1021/acschembio.6c00587">10.1021/acschembio.6c00587</a>.
  short: D. Rohden, F. Napoli, R.J. Lichtenecker, P. Schanda, ACS Chemical Biology
    (2026).
corr_author: '1'
das_tickbox: '1'
dataavailabilitystatement: "Supporting Information is available free of charge at
  https://pubs.acs.org/10.1021/acschembio.6c00587.\r\n\r\nDetailed description of
  experimental methods; spectra supporting the residue assignment for IiMDH; relaxation
  analysis of IiMDH proline-Cδ sites; NMR spectra of isolated [13Cδ,15N,2Hβγ4]-Pro
  (PDF)"
date_created: 2026-10-19T11:12:28Z
date_published: 2026-10-13T00:00:00Z
date_updated: 2026-10-19T11:20:33Z
day: '13'
ddc:
- '540'
department:
- _id: PaSc
- _id: GradSch
doi: 10.1021/acschembio.6c00587
external_id:
  pmid:
  - '42863127'
fulldoi: https://doi.org/10.1021/acschembio.6c00587
has_accepted_license: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1021/acschembio.6c00587
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
  grant_number: I05812
  name: AlloSpace. The emergence and mechanisms of allostery
publication: ACS Chemical Biology
publication_identifier:
  eissn:
  - 1554-8937
  issn:
  - 1554-8929
publication_status: epub_ahead
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Chemoenzymatic proline isotope labeling for solution and magic-angle spinning
  protein nuclear magnetic resonance
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2026'
...