Articles | Volume 2, issue 1
Research article
26 Apr 2021
Research article |  | 26 Apr 2021

Conformational features and ionization states of Lys side chains in a protein studied using the stereo-array isotope labeling (SAIL) method

Mitsuhiro Takeda, Yohei Miyanoiri, Tsutomu Terauchi, and Masatsune Kainosho

Related subject area

Field: Liquid-state NMR | Topic: Applications – biological macromolecules
Facilitating the structural characterisation of non-canonical amino acids in biomolecular NMR
Sarah Kuschert, Martin Stroet, Yanni Ka-Yan Chin, Anne Claire Conibear, Xinying Jia, Thomas Lee, Christian Reinhard Otto Bartling, Kristian Strømgaard, Peter Güntert, Karl Johan Rosengren, Alan Edward Mark, and Mehdi Mobli
Magn. Reson., 4, 57–72,,, 2023
Short summary
Site-selective generation of lanthanoid binding sites on proteins using 4-fluoro-2,6-dicyanopyridine
Sreelakshmi Mekkattu Tharayil, Mithun C. Mahawaththa, Akiva Feintuch, Ansis Maleckis, Sven Ullrich, Richard Morewood, Michael J. Maxwell, Thomas Huber, Christoph Nitsche, Daniella Goldfarb, and Gottfried Otting
Magn. Reson., 3, 169–182,,, 2022
Short summary
Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket
Stephan Grzesiek, Johannes Paladini, Judith Habazettl, and Rajesh Sonti
Magn. Reson., 3, 91–99,,, 2022
Short summary
Localising nuclear spins by pseudocontact shifts from a single tagging site
Henry W. Orton, Elwy H. Abdelkader, Lydia Topping, Stephen J. Butler, and Gottfried Otting
Magn. Reson., 3, 65–76,,, 2022
Short summary
Localising individual atoms of tryptophan side chains in the metallo-β-lactamase IMP-1 by pseudocontact shifts from paramagnetic lanthanoid tags at multiple sites
Henry W. Orton, Iresha D. Herath, Ansis Maleckis, Shereen Jabar, Monika Szabo, Bim Graham, Colum Breen, Lydia Topping, Stephen J. Butler, and Gottfried Otting
Magn. Reson., 3, 1–13,,, 2022
Short summary

Cited articles

André, I., Linse, S., and Mulder, F. A.: Residue-specific pKa determination of lysine and arginine side chains by indirect 15N and 13C NMR spectroscopy: application to apo calmodulin, J. Am. Chem. Soc., 129, 15805–15813,, 2007. 
Barbas III, C. F., Heine, A., Zhong, G., Hoffmann, T., Gramatikova, S., Björnestedt, R., List, B., Anderson, J., Stura, E. A., Wilson, I. A., and Lerner, R. A.: Immune versus natural selection: antibody aldolases with enzymic rates but broader scope, Science, 278, 2085–2092,, 1997. 
Cavanagh, J., Fairbrother, W. J., Palmer, A. G., Rance, M., and Skelton, J. J.: Protein NMR Spectroscopy: Principles and Practice, Academic Press, New York, USA, 2007. 
Chimenti, M. S., Castañeda, C. A., Majumdar, A., and García-Moreno, E. B.: Structural origins of high apparent dielectric constants experienced by ionizable groups in the hydrophobic core of a protein, J. Mol. Biol., 405, 361–377,, 2011. 
Clore, G. M., Bax, A., Driscoll, P. C., Wingfield, P. T., and Gronenborn, A. M.: Assignment of the side chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy, Biochemistry, 29, 8172–8184,, 1990. 
Short summary
Although both the hydrophobic aliphatic chain and hydrophilic ζ-amino group of the lysine side chain presumably contribute to the structures and functions of proteins, the dual nature of the lysine residue has not been fully understood yet, due to the lack of appropriate methods to acquire comprehensive information on its long consecutive methylene chain at the atomic scale. We describe herein a novel strategy to address the current situation using nuclear magnetic resonance spectroscopy.