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Theory and Applications of Biomolecular NMR Spectroscopy

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Biomedical Applications of Biophysics

Part of the book series: Handbook of Modern Biophysics ((HBBT,volume 3))

Abstract

Nuclear magnetic resonance (NMR) spectroscopy is an experimental technique that measures the interaction between electromagnetic radiation and atomic nuclei in atoms and molecules. Atoms bonded to form molecules exist in well-defined nuclear and electronic states (stationary states) that have discrete (quantized) energies. Energy in the form of electromagnetic radiation corresponding to the difference between the energies of the quantized nuclear states can promote the system from one quantum state to another, resulting in either absorption or emission of the radiation. Thus, if the system is going from a state i with energy Ei to a state j with energy Ej, the system changes in energy by an amount ΔEij = Ej – Ei. In NMR spectroscopy, the difference in energy between the quantized nuclear states corresponds to the energy of a radiofrequency photon.

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Authors and Affiliations

  1. Department of Chemistry, University of California Davis, One Shields Avenue, Davis, CA, 95616-8635, USA

    James B. Ames

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  1. Department of Biochemistry and Molecular Medicine, University of California Davis, One Shields Avenue, Davis, CA, 95616, USA

    Thomas Jue Ph.D.

4.1 Electronic Supplementary material

Figure 4.4.

Amino-acid sequence alignment of human KChIP1 (Swiss-Prot accession no. Q9NZI2), mouse DREAM (Q9QXT8), bovine neurocalcin δ (P61602), human hippocalcin (Q5U068), drosophila frequenin (P37236), S. cerevisae Frq1 (Q06389), and bovine recoverin (P21457). The 29-residue EFhand motifs are highlighted in color: EF-1 (green), EF-2 (red), EF-3 (cyan), EF-4 (yellow). Please visit http://extras.springer.com/ to view a high-resolution full-color version of this illustration. (PDF 2,876 KB)

Figure 4.6.

NMR-derived structures of myristoylated recoverin with 0 Ca2+ bound (A), 1 Ca2+ bound (B), and 2 Ca2+ bound (C). The first step of the mechanism involves binding of Ca2+ to EF-3, which causes minor structural changes within the EF-hand that sterically promote a 45° swiveling of the two domains, resulting in partial unclamping of the myristoyl group and dramatic rearrangement at the domain interface. The resulting altered interaction between EF-2 and EF-3 facilitates the binding of a second Ca2+ to the protein at EF-2 in the second step, which causes structural changes within the N-terminal domain that directly lead to ejection of the fatty acyl group. Please visit http://extras.springer.com/ to view a high-resolution full-color version of this illustration. (PDF 2,777 KB)

Figure 4.7.

Mainchain structure (A) and space-filling representation (B) of myristoylated recoverin bound to oriented lipid bilayers determined by solid-state NMR [65]. Hydrophobic residues are yellow, bound Ca2+ ions are orange, and charged residues are red and blue. Please visit http://extras.springer.com/ to view a high-resolution full-color version of this illustration. (PDF 2,785 KB)

Figure 4.8.

Space-filling representations of the Ca2+-bound structures of recoverin (A), frequenin (B), neurocalcin (C), and KChIP1 (D). Exposed hydrophobic residues are yellow, neutral residues are white, and charge residues are red and blue. Please visit http://extras.springer.com/ to view a high-resolution full-color version of this illustration. (PDF 2,838 KB)

Figure 4.9.

Ribbon diagrams illustrating intermolecular interactions for KChIP1 bound to Kv4.2 [69] (A), calmodulin bound to M13 peptide [70] (B), and calcineurin B bound to calcineurin A [72] (C). In each case, a target helix (magenta) is inserted in a groove formed by the helices of EF-1 (green) and EF-2 (red). The intermolecular interactions are mostly hydrophobic, as described in the text. Please visit http://extras.springer.com/ to view a high-resolution full-color version of this illustration. (PDF 2,769 KB)

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Ames, J.B. (2010). Theory and Applications of Biomolecular NMR Spectroscopy. In: Jue, T. (eds) Biomedical Applications of Biophysics. Handbook of Modern Biophysics, vol 3. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60327-233-9_4

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