---
res:
  bibo_abstract:
  - Solid‐state NMR spectroscopy can provide insight into protein structure and dynamics
    at the atomic level without inherent protein size limitations. However, a major
    hurdle to studying large proteins by solid‐state NMR spectroscopy is related to
    spectral complexity and resonance overlap, which increase with molecular weight
    and severely hamper the assignment process. Here the use of two sets of experiments
    is shown to expand the tool kit of 1H‐detected assignment approaches, which correlate
    a given amide pair either to the two adjacent CO–CA pairs (4D hCOCANH/hCOCAcoNH),
    or to the amide 1H of the neighboring residue (3D HcocaNH/HcacoNH, which can be
    extended to 5D). The experiments are based on efficient coherence transfers between
    backbone atoms using INEPT transfers between carbons and cross‐polarization for
    heteronuclear transfers. The utility of these experiments is exemplified with
    application to assemblies of deuterated, fully amide‐protonated proteins from
    approximately 20 to 60 kDa monomer, at magic‐angle spinning (MAS) frequencies
    from approximately 40 to 55 kHz. These experiments will also be applicable to
    protonated proteins at higher MAS frequencies. The resonance assignment of a domain
    within the 50.4 kDa bacteriophage T5 tube protein pb6 is reported, and this is
    compared to NMR assignments of the isolated domain in solution. This comparison
    reveals contacts of this domain to the core of the polymeric tail tube assembly.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Hugo
      foaf_name: Fraga, Hugo
      foaf_surname: Fraga
  - foaf_Person:
      foaf_givenName: Charles‐Adrien
      foaf_name: Arnaud, Charles‐Adrien
      foaf_surname: Arnaud
  - foaf_Person:
      foaf_givenName: Diego F.
      foaf_name: Gauto, Diego F.
      foaf_surname: Gauto
  - foaf_Person:
      foaf_givenName: Maxime
      foaf_name: Audin, Maxime
      foaf_surname: Audin
  - foaf_Person:
      foaf_givenName: Vilius
      foaf_name: Kurauskas, Vilius
      foaf_surname: Kurauskas
  - foaf_Person:
      foaf_givenName: Pavel
      foaf_name: Macek, Pavel
      foaf_surname: Macek
  - foaf_Person:
      foaf_givenName: Carsten
      foaf_name: Krichel, Carsten
      foaf_surname: Krichel
  - foaf_Person:
      foaf_givenName: Jia‐Ying
      foaf_name: Guan, Jia‐Ying
      foaf_surname: Guan
  - foaf_Person:
      foaf_givenName: Jerome
      foaf_name: Boisbouvier, Jerome
      foaf_surname: Boisbouvier
  - foaf_Person:
      foaf_givenName: Remco
      foaf_name: Sprangers, Remco
      foaf_surname: Sprangers
  - foaf_Person:
      foaf_givenName: Cécile
      foaf_name: Breyton, Cécile
      foaf_surname: Breyton
  - 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: 10.1002/cphc.201700572
  bibo_issue: '19'
  bibo_volume: 18
  dct_date: 2017^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/1439-4235
  - http://id.crossref.org/issn/1439-7641
  dct_language: eng
  dct_publisher: Wiley@
  dct_subject:
  - Physical and Theoretical Chemistry
  - Atomic and Molecular Physics
  - and Optics
  dct_title: Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for
    resonance assignment of large proteins@
...