De Novo 3D Structure Determination from Sub-milligram Protein Samples by Solid-State 100 kHz MAS NMR Spectroscopy. Agarwal, V., Penzel, S., Szekely, K., Cadalbert, R., Testori, E., Oss, A., Past, J., Samoson, A., Ernst, M., Böckmann, A., & Meier, B. H Angewandte Chemie (International ed. in English), 53(45):12253–12256, September, 2014. ![De Novo 3D Structure Determination from Sub-milligram Protein Samples by Solid-State 100 kHz MAS NMR Spectroscopy. [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Solid-state NMR spectroscopy is an emerging tool for structural studies of crystalline, membrane-associated, sedimented, and fibrillar proteins. A major limitation for many studies is still the large amount of sample needed for the experiments, typically several isotopically labeled samples of 10-20 mg each. Here we show that a new NMR probe, pushing magic-angle sample rotation to frequencies around 100 kHz, makes it possible to narrow the proton resonance lines sufficiently to provide the necessary sensitivity and spectral resolution for efficient and sensitive proton detection. Using restraints from such spectra, a well-defined de novo structure of the model protein ubiquitin was obtained from two samples of roughly 500 $μ$g protein each. This proof of principle opens new avenues for structural studies of proteins available in microgram, or tens of nanomoles, quantities that are, for example, typically achieved for eukaryotic membrane proteins by in-cell or cell-free expression.
@article{Agarwal2014,
title = {De {Novo} {3D} {Structure} {Determination} from {Sub}-milligram {Protein} {Samples} by {Solid}-{State} 100 {kHz} {MAS} {NMR} {Spectroscopy}.},
volume = {53},
issn = {1521-3773},
url = {http://www.ncbi.nlm.nih.gov/pubmed/25225004},
doi = {10.1002/anie.201405730},
abstract = {Solid-state NMR spectroscopy is an emerging tool for structural studies of crystalline, membrane-associated, sedimented, and fibrillar proteins. A major limitation for many studies is still the large amount of sample needed for the experiments, typically several isotopically labeled samples of 10-20 mg each. Here we show that a new NMR probe, pushing magic-angle sample rotation to frequencies around 100 kHz, makes it possible to narrow the proton resonance lines sufficiently to provide the necessary sensitivity and spectral resolution for efficient and sensitive proton detection. Using restraints from such spectra, a well-defined de novo structure of the model protein ubiquitin was obtained from two samples of roughly 500 \$μ\$g protein each. This proof of principle opens new avenues for structural studies of proteins available in microgram, or tens of nanomoles, quantities that are, for example, typically achieved for eukaryotic membrane proteins by in-cell or cell-free expression.},
number = {45},
journal = {Angewandte Chemie (International ed. in English)},
author = {Agarwal, Vipin and Penzel, Susanne and Szekely, Kathrin and Cadalbert, Riccardo and Testori, Emilie and Oss, Andres and Past, Jaan and Samoson, Ago and Ernst, Matthias and Böckmann, Anja and Meier, Beat H},
month = sep,
year = {2014},
pmid = {25225004},
pages = {12253--12256},
}
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