%0 Journal Article %1 park_resolution_2013 %A Park, Sang Ho %A Yang, Chen %A Opella, Stanley J %A Mueller, Leonard J %D 2013 %J J. Magn. Reson. %K Algorithms,Bacteriophage Isotopes,Nuclear MAS,Glycine,Magnetic Magnetic NMR,Two-dimensional NMR,Variable Pf1,Biomolecular,Capsid Proteins,DNA,Deuterium,Fast Resonance Resonance,Perdeuteration,Pf1 Spectroscopy,Nitrogen bacteriophage,Proteins,Proton contact cross-polarization,Viral detection,Protons,Separated field local spectroscopy,Three-dimensional time %P 164--168 %R 10.1016/j.jmr.2013.10.009 %T Resolution and measurement of heteronuclear dipolar couplings of a noncrystalline protein immobilized in a biological supramolecular assembly by proton-detected \MAS\ solid-state \NMR\ spectroscopy %V 237 %X Two-dimensional (15)N chemical shift/(1)H chemical shift and three-dimensional (1)H-(15)N dipolar coupling/(15)N chemical shift/(1)H chemical shift MAS solid-state NMR correlation spectra of the filamentous bacteriophage Pf1 major coat protein show single-site resolution in noncrystalline, intact-phage preparations. The high sensitivity and resolution result from (1)H detection at 600MHz under 50kHz magic angle spinning using ∼0.5mg of perdeuterated and uniformly (15)N-labeled protein in which the exchangeable amide sites are partially or completely back-exchanged (reprotonated). Notably, the heteronuclear (1)H-(15)N dipolar coupling frequency dimension is shown to select among (15)N resonances, which will be useful in structural studies of larger proteins where the resonances exhibit a high degree of overlap in multidimensional chemical shift correlation spectra.

@article{park_resolution_2013, abstract = {Two-dimensional (15)N chemical shift/(1)H chemical shift and three-dimensional (1)H-(15)N dipolar coupling/(15)N chemical shift/(1)H chemical shift MAS solid-state NMR correlation spectra of the filamentous bacteriophage Pf1 major coat protein show single-site resolution in noncrystalline, intact-phage preparations. The high sensitivity and resolution result from (1)H detection at 600MHz under 50kHz magic angle spinning using ∼0.5mg of perdeuterated and uniformly (15)N-labeled protein in which the exchangeable amide sites are partially or completely back-exchanged (reprotonated). Notably, the heteronuclear (1)H-(15)N dipolar coupling frequency dimension is shown to select among (15)N resonances, which will be useful in structural studies of larger proteins where the resonances exhibit a high degree of overlap in multidimensional chemical shift correlation spectra.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Park, Sang Ho and Yang, Chen and Opella, Stanley J and Mueller, Leonard J}, biburl = {https://www.bibsonomy.org/bibtex/28308e3700c69fdc65279d483caf34592/nmrresource}, doi = {10.1016/j.jmr.2013.10.009}, interhash = {fd17a075b800c04d00548aee6c7753aa}, intrahash = {8308e3700c69fdc65279d483caf34592}, issn = {1096-0856}, journal = {J. Magn. Reson.}, keywords = {Algorithms,Bacteriophage Isotopes,Nuclear MAS,Glycine,Magnetic Magnetic NMR,Two-dimensional NMR,Variable Pf1,Biomolecular,Capsid Proteins,DNA,Deuterium,Fast Resonance Resonance,Perdeuteration,Pf1 Spectroscopy,Nitrogen bacteriophage,Proteins,Proton contact cross-polarization,Viral detection,Protons,Separated field local spectroscopy,Three-dimensional time}, month = dec, pages = {164--168}, pmid = {24225529}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Resolution and measurement of heteronuclear dipolar couplings of a noncrystalline protein immobilized in a biological supramolecular assembly by proton-detected {\{}MAS{\}} solid-state {\{}NMR{\}} spectroscopy}}, volume = 237, year = 2013 }