---
res:
  bibo_abstract:
  - "Understanding enzyme function requires characterizing not only static structure
    but also dynamics and ligand interactions. NMR spectroscopy provides this insight
    at atomic resolution, yet for large proteins the difficulty of resonance assignment
    has largely confined such studies to systems below ∼50 kDa, or to observing only
    methyl groups. Here we present an integrated magic-angle spinning (MAS) and solution
    NMR study of the 134 kDa tetrameric malate dehydrogenase from Ignicoccus islandicus
    (IiMDH), an enzyme of particular interest as an evolutionary intermediate between
    allosteric lactate\r\ndehydrogenases and non-allosteric malate dehydrogenases.
    By combining high-dimensional (up to 4D) MAS NMR experiments on sedimented protein
    with solution NMR, we achieved 92% backbone heavy- atom assignment and 91% assignment
    of all Ile-δ1, Leu-δ1/-δ2, Val-γ1/-γ2, Met-ε and Thr-γ methyl groups. Building
    on these assignments, we use various probes of backbone and sidechain dynamics:
    elevated MAS NMR 15N rotating-frame relaxation (R1ρ) points to microsecond motions
    in functionally critical regions, including the catalytic loop and the mobile
    surface loop. Complementary methyl-axis order parameters from solution NMR identified
    additional flexible sites in the hydrophobic core. Chemical shift perturbation
    experiments upon addition of the substrate analogue oxamate, monitored via backbone
    1H-15N TROSY, revealed both active-site contacts and responses in helices α2F
    and α3G, regions implicated in allosteric signal transmission. The integrated
    approach demonstrated here exploits the distinct strengths of MAS and solution
    NMR, and provides a comprehensive view of structure, dynamics, and substrate interactions
    in a large oligomeric enzyme that would not be accessible by either technique
    alone.@eng"
  bibo_authorlist:
  - 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
  - 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
  bibo_doi: 10.15479/AT-ISTA-22687
  dct_date: 2026^xs_gYear
  dct_publisher: Institute of Science and Technology Austria@
  dct_title: 'Data and scripts for: "Integrated solid/solution NMR assignment allows
    mapping dynamics and ligand binding in a 134 kDa enzyme"@'
...