Abstract
Simple SummaryOxygen is one of the most abundant atoms in the body. Biomolecules, including most proteins, contain a significant number of oxygen atoms, contributing to the maintenance of the structural and functional integrity of biomolecules. Despite these favorable attributes, detailed characterization of these atoms has been challenging, particularly because of the lack of an appropriate analytical tool. Here, we review recent developments in biomolecular 17O nuclear magnetic resonance spectroscopy, which can directly report the physicochemical properties of oxygen atoms in proteins or related biomolecules. We summarize recent studies that successfully employed this technique to elucidate various structural and functional features of proteins and protein complexes. Finally, we discuss a few promising benefits of this methodology, which we believe ensure its further development as a novel and powerful tool for investigating protein structure and folding.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.
Highlights
Our bodies are mainly composed of several biomolecules, including proteins, nucleic acids, polysaccharides, and lipids, along with a large amount of water [1]
X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, cryoelectron microscopy, or their combinatory applications have contributed significantly to our understanding of the structural features of various proteins and protein–biomolecule complexes [4,5,6,7,8]. These techniques complement each other; NMR spectroscopy has a unique position here owing to its evident advantages and limitations [7]
17O NMR spectroscopy with regards to characterization of protein structure and misfoldHerein, we briefly summarize the developments and applications of biomolecular 17 O
Summary
Our bodies are mainly composed of several biomolecules, including proteins, nucleic acids, polysaccharides, and lipids, along with a large amount of water [1]. Recent reconsideration of the theoretical framework of nuclear quadrupole relaxation, along with further advanced instrumental development of NMR methodology, has enabled us to record the solution-state 17 O NMR signals of large biomolecules with sufficient sensitivity and resolution [18,19]. It reaches a maximum at c signal can be narrow under a slow-motion condition, and that it may be ofeasible to obtain ωo τc = 1, and subsequently decreases again in the regime17of ωo τc > > 1 [19] This indicates high-resolution signals for half-integer quadrupolar nuclei, such as O, of a large slowthat the corresponding CT signal can be narrow under a slow-motion condition, and that it tumbling biomolecule, even in an aqueous solution [18,19]. Have been added to studies regarding protein structure and folding
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