[{"external_id":{"pmid":["42057802"]},"tmp":{"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)","image":"/images/cc_by.png"},"date_published":"2026-04-16T00:00:00Z","abstract":[{"text":"The advantageous characteristics attributed to the 19F nucleus have made it a popular target for nuclear magnetic resonance (NMR) once again in recent years. Aside from solution NMR, an increasing number of studies have been conducted applying solid-state magic-angle spinning (MAS) NMR to fluorine-labelled samples. Here, the high chemical shift anisotropy and strong dipolar couplings can be utilised to get structural insights into proteins and measure long distances. Despite increasing popularity and promising benefits, the sensitivity of biomolecular 19F MAS NMR often suffers from slow longitudinal T1 relaxation and therefore long recycle delays. In this work, we expand paramagnetic doping, an approach commonly used to reduce proton T1 relaxation times, to 19F-labelled biological samples. We study the effect of Gd(DTPA) and Gd(DTPA-BMA) on 19F T1 and T2, and 13C T1 and T2 relaxation in a [5-19F13C]-tryptophan-labelled protein via 19F-detected MAS NMR experiments. The observed paramagnetic relaxation enhancement substantially reduces measurement times of 19F MAS NMR experiments without compromising resolution. Additionally, we report the chemical shift assignments of all four fluorotryptophan signals in the 12×39 kDa-large protein TET2 using a mutagenesis approach.","lang":"eng"}],"department":[{"_id":"PaSc"},{"_id":"GradSch"}],"fulldoi":"https://doi.org/10.5194/mr-7-29-2026","pmid":1,"language":[{"iso":"eng"}],"acknowledgement":"We thank Ben P. Tatman for insightful discussions. This research was supported by the Scientific Service Units (SSUs) of ISTA through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility. We thank Prof. Tobias Madl (Medical University Graz) for a sample of Omniscan. Lea M. Becker is the recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria (grant no. PR10660EAW01).","oa_version":"Published Version","PlanS_conform":"1","corr_author":"1","publication_identifier":{"eissn":["2699-0016"]},"publication_status":"published","DOAJ_listed":"1","author":[{"orcid":"0000-0002-6401-5151","last_name":"Becker","full_name":"Becker, Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie"},{"first_name":"Giorgia","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","full_name":"Toscano, Giorgia","last_name":"Toscano"},{"id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna","last_name":"Kapitonova","full_name":"Kapitonova, Anna"},{"full_name":"Singh, Rajkumar","last_name":"Singh","id":"a3089acd-6806-11ee-bacc-f0c7d500ad20","first_name":"Rajkumar"},{"full_name":"Guillerm, Undina","last_name":"Guillerm","first_name":"Undina","id":"bb74f472-ae54-11eb-9835-bc9c22fb1183"},{"last_name":"Lichtenecker","full_name":"Lichtenecker, Roman J.","first_name":"Roman J."},{"first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606"}],"scopus_import":"1","OA_place":"publisher","publisher":"Copernicus Publications","date_updated":"2026-07-20T09:49:12Z","has_accepted_license":"1","volume":7,"year":"2026","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants","main_file_link":[{"open_access":"1","url":"https://doi.org/10.5194/mr-7-29-2026"}],"_id":"21777","publication":"Magnetic Resonance","date_created":"2026-05-03T22:01:36Z","project":[{"name":"IST Austria Open Access Fund","_id":"B67AFEDC-15C9-11EA-A837-991A96BB2854"},{"_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","grant_number":"26777"}],"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"oa":1,"day":"16","article_type":"original","quality_controlled":"1","related_material":{"record":[{"relation":"dissertation_contains","id":"22334","status":"public"}]},"status":"public","citation":{"ama":"Becker LM, Toscano G, Kapitonova A, et al. Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. <i>Magnetic Resonance</i>. 2026;7(1):29-37. doi:<a href=\"https://doi.org/10.5194/mr-7-29-2026\">10.5194/mr-7-29-2026</a>","ista":"Becker LM, Toscano G, Kapitonova A, Singh R, Guillerm U, Lichtenecker RJ, Schanda P. 2026. Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. Magnetic Resonance. 7(1), 29–37.","chicago":"Becker, Lea Marie, Giorgia Toscano, Anna Kapitonova, Rajkumar Singh, Undina Guillerm, Roman J. Lichtenecker, and Paul Schanda. “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” <i>Magnetic Resonance</i>. Copernicus Publications, 2026. <a href=\"https://doi.org/10.5194/mr-7-29-2026\">https://doi.org/10.5194/mr-7-29-2026</a>.","short":"L.M. Becker, G. Toscano, A. Kapitonova, R. Singh, U. Guillerm, R.J. Lichtenecker, P. Schanda, Magnetic Resonance 7 (2026) 29–37.","apa":"Becker, L. M., Toscano, G., Kapitonova, A., Singh, R., Guillerm, U., Lichtenecker, R. J., &#38; Schanda, P. (2026). Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. <i>Magnetic Resonance</i>. Copernicus Publications. <a href=\"https://doi.org/10.5194/mr-7-29-2026\">https://doi.org/10.5194/mr-7-29-2026</a>","ieee":"L. M. Becker <i>et al.</i>, “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants,” <i>Magnetic Resonance</i>, vol. 7, no. 1. Copernicus Publications, pp. 29–37, 2026.","mla":"Becker, Lea Marie, et al. “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” <i>Magnetic Resonance</i>, vol. 7, no. 1, Copernicus Publications, 2026, pp. 29–37, doi:<a href=\"https://doi.org/10.5194/mr-7-29-2026\">10.5194/mr-7-29-2026</a>."},"month":"04","OA_type":"gold","issue":"1","type":"journal_article","intvolume":"         7","doi":"10.5194/mr-7-29-2026","page":"29-37","ddc":["540"],"article_processing_charge":"Yes"},{"citation":{"apa":"Knödlstorfer, S., Toscano, G., Ptaszek, A. L., Kontaxis, G., Napoli, F., Schneider, J., … Konrat, R. (2025). A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">https://doi.org/10.1016/j.jmb.2025.169465</a>","mla":"Knödlstorfer, Sonja, et al. “A Novel HMBC-CC-HMQC NMR Strategy for Methyl Assignment Using Triple-13C-Labeled α-Ketoisovalerate Integrated with UCBShift 2.0.” <i>Journal of Molecular Biology</i>, vol. 437, no. 23, 169465, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">10.1016/j.jmb.2025.169465</a>.","ieee":"S. Knödlstorfer <i>et al.</i>, “A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0,” <i>Journal of Molecular Biology</i>, vol. 437, no. 23. Elsevier, 2025.","ama":"Knödlstorfer S, Toscano G, Ptaszek AL, et al. A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">10.1016/j.jmb.2025.169465</a>","ista":"Knödlstorfer S, Toscano G, Ptaszek AL, Kontaxis G, Napoli F, Schneider J, Maier K, Kapitonova A, Lichtenecker RJ, Schanda P, Konrat R. 2025. A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. Journal of Molecular Biology. 437(23), 169465.","short":"S. Knödlstorfer, G. Toscano, A.L. Ptaszek, G. Kontaxis, F. Napoli, J. Schneider, K. Maier, A. Kapitonova, R.J. Lichtenecker, P. Schanda, R. Konrat, Journal of Molecular Biology 437 (2025).","chicago":"Knödlstorfer, Sonja, Giorgia Toscano, Aleksandra L. Ptaszek, Georg Kontaxis, Federico Napoli, Jakob Schneider, Katharina Maier, et al. “A Novel HMBC-CC-HMQC NMR Strategy for Methyl Assignment Using Triple-13C-Labeled α-Ketoisovalerate Integrated with UCBShift 2.0.” <i>Journal of Molecular Biology</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">https://doi.org/10.1016/j.jmb.2025.169465</a>."},"month":"12","OA_type":"hybrid","status":"public","type":"journal_article","issue":"23","article_number":"169465","intvolume":"       437","doi":"10.1016/j.jmb.2025.169465","ddc":["540"],"article_processing_charge":"Yes (in subscription journal)","title":"A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2025-10-26T23:01:35Z","file_date_updated":"2025-12-30T10:29:08Z","_id":"20538","publication":"Journal of Molecular Biology","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"project":[{"grant_number":"I06223","_id":"bdb9578d-d553-11ed-ba76-ed5d39fce6f0","name":"Structure and mechanism of the mitochondrial MIM insertase"},{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812"}],"quality_controlled":"1","day":"01","article_type":"original","oa":1,"oa_version":"Published Version","PlanS_conform":"1","publication_identifier":{"issn":["0022-2836"],"eissn":["1089-8638"]},"publication_status":"published","OA_place":"publisher","scopus_import":"1","author":[{"first_name":"Sonja","last_name":"Knödlstorfer","full_name":"Knödlstorfer, Sonja"},{"first_name":"Giorgia","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","last_name":"Toscano","full_name":"Toscano, Giorgia"},{"last_name":"Ptaszek","full_name":"Ptaszek, Aleksandra L.","first_name":"Aleksandra L."},{"first_name":"Georg","full_name":"Kontaxis, Georg","last_name":"Kontaxis"},{"full_name":"Napoli, Federico","last_name":"Napoli","orcid":"0000-0002-9043-136X","first_name":"Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b"},{"id":"64368429-eb97-11eb-a6c2-c980b1f44415","first_name":"Jakob","full_name":"Schneider, Jakob","last_name":"Schneider"},{"last_name":"Maier","full_name":"Maier, Katharina","first_name":"Katharina"},{"full_name":"Kapitonova, Anna","last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna"},{"first_name":"Roman J.","full_name":"Lichtenecker, Roman J.","last_name":"Lichtenecker"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul"},{"first_name":"Robert","full_name":"Konrat, Robert","last_name":"Konrat"}],"date_updated":"2026-08-13T14:19:02Z","has_accepted_license":"1","publisher":"Elsevier","year":"2025","volume":437,"file":[{"file_size":3076611,"creator":"dernst","content_type":"application/pdf","success":1,"date_updated":"2025-12-30T10:29:08Z","file_id":"20915","access_level":"open_access","date_created":"2025-12-30T10:29:08Z","checksum":"feb92f9c79032c261165f4ca573f444a","relation":"main_file","file_name":"2025_JourMolecularBiology_Knoedlstorfer.pdf"}],"external_id":{"pmid":["41016549"]},"tmp":{"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)","image":"/images/cc_by.png"},"date_published":"2025-12-01T00:00:00Z","department":[{"_id":"PaSc"},{"_id":"GradSch"}],"abstract":[{"lang":"eng","text":"In this study, we describe an integrated approach for methyl group assignment comprising precursor-based selective methyl group labeling, a novel pulse sequence for methyl to backbone coherence transfer and chemical shift predictions using UCBShift 2.0. The utility of this novel α-ketoacid isotopologue is shown by the adaptation of an HMBC-HMQC pulse sequence that simultaneously connects geminal methyl groups of leucine and valine residues to each other and to the protein backbone. By additional 13C,2H-labeling of residues other than valine and leucine residues of the protein, important chemical shift information about neighboring residues (following valine and leucine residues) can be achieved. Thus, different valine and leucine residues in a protein can be characterized as a specific chemical shift vector. Frequency matching with predicted chemical shifts via UCBShift 2.0 using experimental data taken from a subset of the BMRB database revealed a correct assignment performance of about 90%. With applications to proteins of 60.2 kDa and 134 kDa (4 × 33.5 kDa) in size, we demonstrate that the approach provides valuable information even for very large proteins."}],"fulldoi":"https://doi.org/10.1016/j.jmb.2025.169465","acknowledgement":"A.L.P and G.T were funded by the “New Ideas” program by Vienna Doctoral School in Chemistry. S.K. was funded by the Austrian Science Fund FWF P35098-B. This work was supported financially by the Austrian Science Fund (FWF, grant numbers I06223 and I5812-B, “AlloSpace”). This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility (LSF). We thank Celina Sailer for assistance with the analysis of the NMR spectrum of HsTom70.","language":[{"iso":"eng"}],"pmid":1}]