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17O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding

Title
17O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding
Authors
Muniyappan, SrinivasanLin, YuxiLee, Young-HoKim, Jin Hae
DGIST Authors
Muniyappan, Srinivasan; Lin, Yuxi; Lee, Young-Ho; Kim, Jin Hae
Issue Date
2021-05
Citation
Biology, 10(6), 453
Type
Article
Author Keywords
O-17 NMR spectroscopyprotein structuresprotein foldingoxygen-17
Keywords
SOLID-STATE NMRNUCLEAR-MAGNETIC-RESONANCEX-RAY CRYSTALLOGRAPHYNEUTRON CRYSTALLOGRAPHYCRYOELECTRON MICROSCOPYBIOLOGICAL MOLECULESQUADRUPOLAR NUCLEICRYO-EMRESOLUTIONWATER
ISSN
2079-7737
Abstract
Oxygen is a key atom that maintains biomolecular structures, regulates various physiological processes, and mediates various biomolecular interactions. Oxygen-17 (17O), 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) 17O 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 17O NMR spectroscopic investigations of biomolecules have been considerably hampered due to low natural abundance and the quadruple characteristics of the 17O 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 17O 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.
URI
http://hdl.handle.net/20.500.11750/15443
DOI
10.3390/biology10060453
Publisher
Multidisciplinary Digital Publishing Institute (MDPI)
Related Researcher
Files:
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Collection:
Department of New BiologyProtein Structure Aging Laboratory1. Journal Articles


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