Abstract
Application of nuclear magnetic resonance (NMR) in protein studies is briefly described. The basic physical principles of the method are introduced, and relation of NMR spectra to chemical structure is explained. The basic technique of isotope labeling is presented, and recommendations for sample preparations are reviewed. The methods used for assignment of NMR spectra, structure determinations, investigation of intermolecular interactions, and monitoring molecular motions are discussed.
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Notes
- 1.
A promising possibility of improving the sensitivity is dynamic nuclear polarization, taking advantage of a much larger difference between the energies of magnetic moments of unpaired electrons.
- 2.
In practice, the correlation with the carbons of the preceding amino acid is often observed too because the one-bond and two-bond 15N-13Cα interactions are of similar strength.
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Financial contribution made by the Ministry of Education, Youths, and Sports of the Czech Republic within special support paid from the National Programme for Sustainability II funds, project CEITEC 2020 (LQ1601), is gratefully acknowledged.
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Zachrdla, M., Jaseňáková, Z., Žídek, L. (2018). Nuclear Magnetic Resonance. In: Hejátko, J., Hakoshima, T. (eds) Plant Structural Biology: Hormonal Regulations. Springer, Cham. https://doi.org/10.1007/978-3-319-91352-0_12
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