<sup>17</sup>O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding
Oxygen is a key atom that maintains biomolecular structures, regulates various physiological processes, and mediates various biomolecular interactions. Oxygen-17 (<sup>17</sup>O), therefore, has been proposed as a useful probe that can provide detailed information about various physicoch...
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| Format: | Article |
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MDPI AG
2021-05-01
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| Online Access: | https://www.mdpi.com/2079-7737/10/6/453 |
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| author | Srinivasan Muniyappan Yuxi Lin Young-Ho Lee Jin Hae Kim |
| author_facet | Srinivasan Muniyappan Yuxi Lin Young-Ho Lee Jin Hae Kim |
| author_sort | Srinivasan Muniyappan |
| collection | DOAJ |
| description | Oxygen is a key atom that maintains biomolecular structures, regulates various physiological processes, and mediates various biomolecular interactions. Oxygen-17 (<sup>17</sup>O), therefore, has been proposed as a useful probe that can provide detailed information about various physicochemical features of proteins. This is attributed to the facts that (1) <sup>17</sup>O is an active isotope for nuclear magnetic resonance (NMR) spectroscopic approaches; (2) NMR spectroscopy is one of the most suitable tools for characterizing the structural and dynamical features of biomolecules under native-like conditions; and (3) oxygen atoms are frequently involved in essential hydrogen bonds for the structural and functional integrity of proteins or related biomolecules. Although <sup>17</sup>O NMR spectroscopic investigations of biomolecules have been considerably hampered due to low natural abundance and the quadruple characteristics of the <sup>17</sup>O nucleus, recent theoretical and technical developments have revolutionized this methodology to be optimally poised as a unique and widely applicable tool for determining protein structure and dynamics. In this review, we recapitulate recent developments in <sup>17</sup>O NMR spectroscopy to characterize protein structure and folding. In addition, we discuss the highly promising advantages of this methodology over other techniques and explain why further technical and experimental advancements are highly desired. |
| first_indexed | 2024-03-10T11:11:19Z |
| format | Article |
| id | doaj.art-6cec45af39cd45b48ca03b89ad59da3a |
| institution | Directory Open Access Journal |
| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-10T11:11:19Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
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| spelling | doaj.art-6cec45af39cd45b48ca03b89ad59da3a2023-11-21T20:46:31ZengMDPI AGBiology2079-77372021-05-0110645310.3390/biology10060453<sup>17</sup>O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and FoldingSrinivasan Muniyappan0Yuxi Lin1Young-Ho Lee2Jin Hae Kim3Department of New Biology, Daegu Gyeongbuk Institute of Science and Technology (DGIST), Daegu 42988, KoreaResearch Center for Bioconvergence Analysis, Korea Basic Science Institute, Cheongju 28119, KoreaResearch Center for Bioconvergence Analysis, Korea Basic Science Institute, Cheongju 28119, KoreaDepartment of New Biology, Daegu Gyeongbuk Institute of Science and Technology (DGIST), Daegu 42988, KoreaOxygen is a key atom that maintains biomolecular structures, regulates various physiological processes, and mediates various biomolecular interactions. Oxygen-17 (<sup>17</sup>O), therefore, has been proposed as a useful probe that can provide detailed information about various physicochemical features of proteins. This is attributed to the facts that (1) <sup>17</sup>O is an active isotope for nuclear magnetic resonance (NMR) spectroscopic approaches; (2) NMR spectroscopy is one of the most suitable tools for characterizing the structural and dynamical features of biomolecules under native-like conditions; and (3) oxygen atoms are frequently involved in essential hydrogen bonds for the structural and functional integrity of proteins or related biomolecules. Although <sup>17</sup>O NMR spectroscopic investigations of biomolecules have been considerably hampered due to low natural abundance and the quadruple characteristics of the <sup>17</sup>O nucleus, recent theoretical and technical developments have revolutionized this methodology to be optimally poised as a unique and widely applicable tool for determining protein structure and dynamics. In this review, we recapitulate recent developments in <sup>17</sup>O NMR spectroscopy to characterize protein structure and folding. In addition, we discuss the highly promising advantages of this methodology over other techniques and explain why further technical and experimental advancements are highly desired.https://www.mdpi.com/2079-7737/10/6/453<sup>17</sup>O NMR spectroscopyprotein structuresprotein foldingoxygen-17 |
| spellingShingle | Srinivasan Muniyappan Yuxi Lin Young-Ho Lee Jin Hae Kim <sup>17</sup>O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding Biology <sup>17</sup>O NMR spectroscopy protein structures protein folding oxygen-17 |
| title | <sup>17</sup>O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding |
| title_full | <sup>17</sup>O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding |
| title_fullStr | <sup>17</sup>O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding |
| title_full_unstemmed | <sup>17</sup>O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding |
| title_short | <sup>17</sup>O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding |
| title_sort | sup 17 sup o nmr spectroscopy a novel probe for characterizing protein structure and folding |
| topic | <sup>17</sup>O NMR spectroscopy protein structures protein folding oxygen-17 |
| url | https://www.mdpi.com/2079-7737/10/6/453 |
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