@article{Sergeyev2017,
	title = {Efficient assignment and {NMR} analysis of an intact virus using sequential side-chain correlations and {DNP} sensitization.},
	volume = {114},
	issn = {1091-6490},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/28461483},
	doi = {10.1073/pnas.1701484114},
	abstract = {An experimental strategy has been developed to increase the efficiency of dynamic nuclear polarization (DNP) in solid-state NMR studies. The method makes assignments simpler, faster, and more reliable via sequential correlations of both side-chain and C\$α\$ resonances. The approach is particularly suited to complex biomolecules and systems with significant chemical-shift degeneracy. It was designed to overcome the spectral congestion and line broadening that occur due to sample freezing at the cryogenic temperatures required for DNP. Nonuniform sampling (NUS) is incorporated to achieve time-efficient collection of multidimensional data. Additionally, fast (25 kHz) magic-angle spinning (MAS) provides optimal sensitivity and resolution. Data collected in {\textless}1 wk produced a virtually complete de novo assignment of the coat protein of Pf1 virus. The peak positions and linewidths for samples near 100 K are perturbed relative to those near 273 K. These temperature-induced perturbations are strongly correlated with hydration surfaces.},
	number = {20},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	author = {Sergeyev, Ivan V and Itin, Boris and Rogawski, Rivkah and Day, Loren A and McDermott, Ann E},
	month = may,
	year = {2017},
	pmid = {28461483},
	note = {Publisher: National Academy of Sciences},
	keywords = {DNP, Pf1 bacteriophage, SSNMR},
	pages = {5171--5176},
}

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It was designed to overcome the spectral congestion and line broadening that occur due to sample freezing at the cryogenic temperatures required for DNP. Nonuniform sampling (NUS) is incorporated to achieve time-efficient collection of multidimensional data. Additionally, fast (25 kHz) magic-angle spinning (MAS) provides optimal sensitivity and resolution. Data collected in \\textless1 wk produced a virtually complete de novo assignment of the coat protein of Pf1 virus. The peak positions and linewidths for samples near 100 K are perturbed relative to those near 273 K. These temperature-induced perturbations are strongly correlated with hydration surfaces.","number":"20","journal":"Proceedings of the National Academy of Sciences of the United States of America","author":[{"propositions":[],"lastnames":["Sergeyev"],"firstnames":["Ivan","V"],"suffixes":[]},{"propositions":[],"lastnames":["Itin"],"firstnames":["Boris"],"suffixes":[]},{"propositions":[],"lastnames":["Rogawski"],"firstnames":["Rivkah"],"suffixes":[]},{"propositions":[],"lastnames":["Day"],"firstnames":["Loren","A"],"suffixes":[]},{"propositions":[],"lastnames":["McDermott"],"firstnames":["Ann","E"],"suffixes":[]}],"month":"May","year":"2017","pmid":"28461483","note":"Publisher: National Academy of Sciences","keywords":"DNP, Pf1 bacteriophage, SSNMR","pages":"5171–5176","bibtex":"@article{Sergeyev2017,\n\ttitle = {Efficient assignment and {NMR} analysis of an intact virus using sequential side-chain correlations and {DNP} sensitization.},\n\tvolume = {114},\n\tissn = {1091-6490},\n\turl = {http://www.ncbi.nlm.nih.gov/pubmed/28461483},\n\tdoi = {10.1073/pnas.1701484114},\n\tabstract = {An experimental strategy has been developed to increase the efficiency of dynamic nuclear polarization (DNP) in solid-state NMR studies. The method makes assignments simpler, faster, and more reliable via sequential correlations of both side-chain and C\\$α\\$ resonances. The approach is particularly suited to complex biomolecules and systems with significant chemical-shift degeneracy. It was designed to overcome the spectral congestion and line broadening that occur due to sample freezing at the cryogenic temperatures required for DNP. Nonuniform sampling (NUS) is incorporated to achieve time-efficient collection of multidimensional data. Additionally, fast (25 kHz) magic-angle spinning (MAS) provides optimal sensitivity and resolution. Data collected in {\\textless}1 wk produced a virtually complete de novo assignment of the coat protein of Pf1 virus. The peak positions and linewidths for samples near 100 K are perturbed relative to those near 273 K. 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