Protein deuteration via algal amino acids to circumvent proton back-exchange for 1H-detected solid-state NMR
| dc.contributor.author | Aucharova, Hanna | |
| dc.contributor.author | Klein, Alexander | |
| dc.contributor.author | Medina Gomez, Sara | |
| dc.contributor.author | Söldner, Benedikt | |
| dc.contributor.author | Vasa, Suresh K. | |
| dc.contributor.author | Linser, Rasmus | |
| dc.date.accessioned | 2025-09-09T12:49:13Z | |
| dc.date.available | 2025-09-09T12:49:13Z | |
| dc.date.issued | 2024-02-21 | |
| dc.description.abstract | With perdeuteration, solid-state NMR spectroscopy of large proteins suffers from incomplete amide-proton back-exchange. Using a 72 kDa micro-crystalline protein, we show that deuteration exclusively via deuterated amino acids, well-established in solution to suppress sidechain protonation without proton back-exchange obstacles, provides spectral resolution comparable to perdeuterated preparations at intermediate spinning frequencies. | en |
| dc.identifier.uri | http://hdl.handle.net/2003/43873 | |
| dc.language.iso | en | |
| dc.relation.ispartofseries | Chemical communications; 60(22) | |
| dc.rights.uri | http://creativecommons.org/licenses/by/3.0/ | |
| dc.subject.ddc | 540 | |
| dc.title | Protein deuteration via algal amino acids to circumvent proton back-exchange for 1H-detected solid-state NMR | en |
| dc.type | Text | |
| dc.type.publicationtype | Article | |
| dcterms.accessRights | open access | |
| eldorado.doi.register | false | |
| eldorado.secondarypublication | true | |
| eldorado.secondarypublication.primarycitation | Aucharova, H., Klein, A., Medina Gomez, S., Söldner, B., Vasa, S. K., & Linser, R. (2024). Protein deuteration via algal amino acids to circumvent proton back-exchange for 1H-detected solid-state NMR. Chemical Communications, 60(22), 3083–3086. https://doi.org/10.1039/d4cc00213j | |
| eldorado.secondarypublication.primaryidentifier | https://doi.org/10.1039/D4CC00213J |