Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping ¹³C chemical shift ranges between 100 and 160 ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet aromatic residues play...
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| Format: | Article |
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Elsevier
2018
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| Online Access: | http://hdl.handle.net/1721.1/113323 https://orcid.org/0000-0002-7272-6885 https://orcid.org/0000-0001-5255-5858 |
| _version_ | 1826209426871156736 |
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| author | Schmidt-Rohr, Klaus Williams, Jonathan Kyle Hong, Mei |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Schmidt-Rohr, Klaus Williams, Jonathan Kyle Hong, Mei |
| author_sort | Schmidt-Rohr, Klaus |
| collection | MIT |
| description | The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping ¹³C chemical shift ranges between 100 and 160 ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet aromatic residues play important roles in biology through π-π and cation-π interactions. To better resolve and assign aromatic residues' ¹³C signals in magic-angle-spinning (MAS) solid-state NMR spectra, we introduce two spectral editing techniques. The first method uses gated ¹H decoupling in a proton-driven spin-diffusion (PDSD) experiment to remove all protonated ¹³C signals and retain only non-protonated carbon signals in the aromatic region of the ¹³C spectra. The second technique uses chemical shift filters and ¹H-¹³C dipolar dephasing to selectively detect the Cα, Cβ and CO cross peaks of aromatic residues while suppressing the signals of all aliphatic residues. We demonstrate these two techniques on amino acids, a model peptide, and the microcrystalline protein GB1, and show that they significantly simplify the 2D NMR spectra and both reveal and permit the ready assignment of the aromatic residues' signals. |
| first_indexed | 2024-09-23T14:22:40Z |
| format | Article |
| id | mit-1721.1/113323 |
| institution | Massachusetts Institute of Technology |
| last_indexed | 2024-09-23T14:22:40Z |
| publishDate | 2018 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | mit-1721.1/1133232022-10-01T20:55:05Z Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins Schmidt-Rohr, Klaus Williams, Jonathan Kyle Hong, Mei Massachusetts Institute of Technology. Department of Chemistry Williams, Jonathan Kyle Hong, Mei The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping ¹³C chemical shift ranges between 100 and 160 ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet aromatic residues play important roles in biology through π-π and cation-π interactions. To better resolve and assign aromatic residues' ¹³C signals in magic-angle-spinning (MAS) solid-state NMR spectra, we introduce two spectral editing techniques. The first method uses gated ¹H decoupling in a proton-driven spin-diffusion (PDSD) experiment to remove all protonated ¹³C signals and retain only non-protonated carbon signals in the aromatic region of the ¹³C spectra. The second technique uses chemical shift filters and ¹H-¹³C dipolar dephasing to selectively detect the Cα, Cβ and CO cross peaks of aromatic residues while suppressing the signals of all aliphatic residues. We demonstrate these two techniques on amino acids, a model peptide, and the microcrystalline protein GB1, and show that they significantly simplify the 2D NMR spectra and both reveal and permit the ready assignment of the aromatic residues' signals. National Institutes of Health (U.S.) (Grant GM088204) 2018-01-29T16:15:13Z 2018-01-29T16:15:13Z 2015-09 2015-09 2018-01-26T13:20:42Z Article http://purl.org/eprint/type/JournalArticle 0926-2040 http://hdl.handle.net/1721.1/113323 Williams, Jonathan K. et al. “Aromatic Spectral Editing Techniques for Magic-Angle-Spinning Solid-State NMR Spectroscopy of Uniformly ¹³C-Labeled Proteins.” Solid State Nuclear Magnetic Resonance 72 (November 2015): 118–126. © 2015 Elsevier Inc https://orcid.org/0000-0002-7272-6885 https://orcid.org/0000-0001-5255-5858 http://dx.doi.org/10.1016/J.SSNMR.2015.09.006 Solid State Nuclear Magnetic Resonance Creative Commons Attribution-NonCommercial-NoDerivs License http://creativecommons.org/licenses/by-nc-nd/4.0/ application/pdf Elsevier PMC |
| spellingShingle | Schmidt-Rohr, Klaus Williams, Jonathan Kyle Hong, Mei Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins |
| title | Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins |
| title_full | Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins |
| title_fullStr | Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins |
| title_full_unstemmed | Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins |
| title_short | Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins |
| title_sort | aromatic spectral editing techniques for magic angle spinning solid state nmr spectroscopy of uniformly 13c labeled proteins |
| url | http://hdl.handle.net/1721.1/113323 https://orcid.org/0000-0002-7272-6885 https://orcid.org/0000-0001-5255-5858 |
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