Synonyms
Definition
J or scalar coupling between magnetic nuclei (otherwise termed nuclear spins) is coupling via the intervening network of chemical bonds and depends on interaction between the nuclear spins and bonding electron spins.
Introduction
J or scalar coupling occurs between magnetic nuclei that are chemically bonded to one another (Cavanagh et al. 2007; Hore 1995; Rule and Hitchens 2006). Scalar coupling is important because many NMR pulse sequences used to investigate molecular structure, dynamics, and interactions depend on scalar coupling for magnetization transfer between nuclear spins. Scalar coupling, moreover, allows delineation of the chemical connectivity and stereochemistry within a molecule, be it a small molecule or biological macromolecule; together with through-space dipolar coupling, therefore, through-bond scalar coupling forms the basis of resonance assignment and NMR determination of 3D structures of molecules. Here I...
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References
Barnwal RP, Rout AK, Chary KVR, Atreya HS. Rapid measurement of 3J(HN-Hα) and 3(N-Hβ) coupling constants in polypeptides. J Biomol NMR. 2007;39:259–63.
Bax A, Vuister GW, Grzesiek S, Delaglio F, Wang AC, Tschudin R, Zhu G. Measurement of homonuclear and heteronuclear J-couplings from quantitative J-correlation. In: Abelson JN, Simon MI, James TL, Oppenheimer NJ, editors. Methods in enzymology: nuclear magnetic resonance, Pt C. San Diego: Academic; 1994. p. 79–105.
Billeter M, Neri D, Otting G, Qian YQ, Wüthrich K. Precise vicinal coupling-constants 3JHNα in proteins from nonlinear fits of J-modulated [15N-1H]-COSY experiments. J Biomol NMR. 1992;2:257–74.
Boehr DD, Nussinov R, Wright PE. The role of dynamic conformational ensembles in biomolecular recognition. Nature Chem Biol. 2009;5:789–96.
Cavanagh J, Fairbrother WJ, Palmer III AG, Rance M, Skelton NJ. Protein NMR spectroscopy: principles and practice. Boston: Academic; 2007.
Evans JNS. Biomolecular NMR spectroscopy. Oxford: Oxford University Press; 1995.
Freeman R. Spin choreography: basic steps in high resolution NMR. Oxford: Oxford University Press; 1997.
Grzesiek S, Cordier F, Jaravine V, Barfield M. Insights into biomolecular hydrogen bonds from hydrogen bond scalar couplings. Prog Nucl Magn Reson Spectrosc. 2004;45:275–300.
Habazettl J, Allan MG, Jenal U, Grzesiek S. Solution structure of the PilZ domain protein PA4608 complex with cyclic di-GMP identifies charge clustering as molecular readout. J Biol Chem. 2011;286:14304–14.
Hahnke MJ, Richter C, Heinicke F, Schwalbe H. The HN(COCA)HAHB NMR experiment for the stereospecific assignment of Hβ-protons in non-native states of proteins. J Am Chem Soc. 2010;132:918–19.
Hore PJ. Nuclear magnetic resonance. Oxford: Oxford University Press; 1995.
Lendel C, Damberg P. 3D J-resolved NMR spectroscopy for unstructured polypeptides: fast measurement of 3JHNHα coupling constants with outstanding spectral resolution. J Biomol NMR. 2009;44:35–42.
Liu YZ, Prestegard JH. Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments. J Magn Reson. 2009;200:109–18.
Löhr F, Reckel S, Stefer S, Dötsch V, Schmidt J. Improved accuracy in measuring one-bond and two-bond 15N,13Cα coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy. J Biomol NMR. 2011;50:167–90.
Markwick PRL, Showalter SA, Bouvignies G, Brüschweiler R, Blackledge M. Structural dynamics of protein backbone phi angles: extended molecular dynamics simulations versus experimental 3J scalar couplings. J Biomol NMR. 2009;45:17–21.
Nozinovic S, Fürtig B, Jonker HR, Richter C, Schwalbe H. High-resolution NMR structure of an RNA model system: the 14-mer cUUCGg tetraloop hairpin RNA. Nucleic Acids Res. 2010;38:683–94.
Otten R, Wood K, Mulder FAA. Comprehensive determination of 3JHNHα for unfolded proteins using 13C′-resolved spin-echo difference spectroscopy. J Biomol NMR. 2009;45:343–9.
Permi P, Annila A. Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings. J Biomol NMR. 2000;16:221–7.
Rule GS, Hitchens TK. Fundamentals of protein NMR spectroscopy. Dordrecht: Springer; 2006.
Sass HJ, Schmid FFF, Grzesiek S. Correlation of protein structure and dynamics to scalar couplings across hydrogen bonds. J Am Chem Soc. 2007;129:5898–903.
Schmidt JM, Howard MJ, Maestre-Martinez M, Pérez CS, Löhr F. Variation in protein Cα-related one-bond J couplings. Magn Reson Chem. 2009;47:16–30.
Schmidt JM, Hua Y, Löhr F. Correlation of 2J couplings with protein secondary structure. Proteins-Struct Funct Bioinform. 2010;78:1544–62.
Schmidt JM, Zhou S, Rowe ML, Howard MJ, Williamson RA, Löhr F. One-bond and two-bond J couplings help annotate protein secondary-structure motifs: J-coupling indexing applied to human endoplasmic reticulum protein ERp18. Proteins-Struct Funct Bioinform. 2011;79:428–43.
Vuister GW, Tessari M, Karimi-Nejad Y, Whitehead B. Pulse sequences for measuring coupling constants. In: Krishna NR, Berliner LJ, editors. Modern techniques in protein NMR. New York: Kluwer; 1999. p. 195–257.
Zandarashvili L, Li D-W, Wang T, Brüschweiler R, Iwahara J. Signature of mobile hydrogen bonding of lysine side chains from long-range 15N–13C scalar J-couplings and computation. J Am Chem Soc. 2011;133:9192–5.
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Bagby, S. (2013). J Coupling. In: Roberts, G.C.K. (eds) Encyclopedia of Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16712-6_306
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DOI: https://doi.org/10.1007/978-3-642-16712-6_306
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