TY - JOUR
T1 - 17o nmr spectroscopy
T2 - A novel probe for characterizing protein structure and folding
AU - Muniyappan, Srinivasan
AU - Lin, Yuxi
AU - Lee, Young Ho
AU - Kim, Jin Hae
N1 - Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2021/5/21
Y1 - 2021/5/21
N2 - 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. Although17O NMR spectroscopic investi-gations of biomolecules have been considerably hampered due to low natural abundance and the quadruple characteristics of the17O 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 in17O 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.
AB - 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. Although17O NMR spectroscopic investi-gations of biomolecules have been considerably hampered due to low natural abundance and the quadruple characteristics of the17O 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 in17O 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.
KW - 17O NMR spectroscopy
KW - Oxygen-17
KW - Protein folding
KW - Protein structures
UR - http://www.scopus.com/inward/record.url?scp=85107231675&partnerID=8YFLogxK
U2 - 10.3390/biology10060453
DO - 10.3390/biology10060453
M3 - Article
AN - SCOPUS:85107231675
SN - 2079-7737
VL - 10
JO - Biology
JF - Biology
IS - 6
M1 - 453
ER -