--- _id: '8446' abstract: - lang: eng text: 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. article_processing_charge: No article_type: original author: - first_name: Hugo full_name: Fraga, Hugo last_name: Fraga - first_name: Charles‐Adrien full_name: Arnaud, Charles‐Adrien last_name: Arnaud - first_name: Diego F. full_name: Gauto, Diego F. last_name: Gauto - first_name: Maxime full_name: Audin, Maxime last_name: Audin - first_name: Vilius full_name: Kurauskas, Vilius last_name: Kurauskas - first_name: Pavel full_name: Macek, Pavel last_name: Macek - first_name: Carsten full_name: Krichel, Carsten last_name: Krichel - first_name: Jia‐Ying full_name: Guan, Jia‐Ying last_name: Guan - first_name: Jerome full_name: Boisbouvier, Jerome last_name: Boisbouvier - first_name: Remco full_name: Sprangers, Remco last_name: Sprangers - first_name: Cécile full_name: Breyton, Cécile last_name: Breyton - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Fraga H, Arnaud C, Gauto DF, et al. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. 2017;18(19):2697-2703. doi:10.1002/cphc.201700572 apa: Fraga, H., Arnaud, C., Gauto, D. F., Audin, M., Kurauskas, V., Macek, P., … Schanda, P. (2017). Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201700572 chicago: Fraga, Hugo, Charles‐Adrien Arnaud, Diego F. Gauto, Maxime Audin, Vilius Kurauskas, Pavel Macek, Carsten Krichel, et al. “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.” ChemPhysChem. Wiley, 2017. https://doi.org/10.1002/cphc.201700572. ieee: H. Fraga et al., “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins,” ChemPhysChem, vol. 18, no. 19. Wiley, pp. 2697–2703, 2017. ista: Fraga H, Arnaud C, Gauto DF, Audin M, Kurauskas V, Macek P, Krichel C, Guan J, Boisbouvier J, Sprangers R, Breyton C, Schanda P. 2017. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. 18(19), 2697–2703. mla: Fraga, Hugo, et al. “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.” ChemPhysChem, vol. 18, no. 19, Wiley, 2017, pp. 2697–703, doi:10.1002/cphc.201700572. short: H. Fraga, C. Arnaud, D.F. Gauto, M. Audin, V. Kurauskas, P. Macek, C. Krichel, J. Guan, J. Boisbouvier, R. Sprangers, C. Breyton, P. Schanda, ChemPhysChem 18 (2017) 2697–2703. date_created: 2020-09-18T10:06:09Z date_published: 2017-08-09T00:00:00Z date_updated: 2021-01-12T08:19:19Z day: '09' doi: 10.1002/cphc.201700572 extern: '1' intvolume: ' 18' issue: '19' keyword: - Physical and Theoretical Chemistry - Atomic and Molecular Physics - and Optics language: - iso: eng month: '08' oa_version: None page: 2697-2703 publication: ChemPhysChem publication_identifier: issn: - 1439-4235 - 1439-7641 publication_status: published publisher: Wiley quality_controlled: '1' status: public title: Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 18 year: '2017' ...