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Review
.2018:1688:1-35.
doi: 10.1007/978-1-4939-7386-6_1.

NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology

Affiliations
Review

NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology

Caitlin M Quinn et al. Methods Mol Biol.2018.

Abstract

As a result of profound gains in sensitivity and resolution afforded by ultrahigh magnetic fields, transformative applications in the fields of structural biology and materials science are being realized. The development of dual low temperature superconducting (LTS)/high-temperature superconducting (HTS) magnets has enabled the achievement of magnetic fields above 1 GHz (23.5 T), which will open doors to an unprecedented new range of applications. In this contribution, we discuss the promise of ultrahigh field magnetic resonance. We highlight several methodological developments pertinent at high-magnetic fields including measurement of1H-1H distances and1H chemical shift anisotropy in the solid state as well as studies of quadrupolar nuclei such as17O. Higher magnetic fields have advanced heteronuclear detection in solution NMR, valuable for applications including metabolomics and disordered proteins, as well as expanded use of proton detection in the solid state in conjunction with ultrafast magic angle spinning. We also present several recent applications to structural studies of the AP205 bacteriophage, the M2 channel from Influenza A, and biomaterials such as human bone. Gains in sensitivity and resolution from increased field strengths will enable advanced applications of NMR spectroscopy including in vivo studies of whole cells and intact virions.

Keywords: Biomaterials; Fast magic angle spinning; Nonuniform sampling; Proton detection; Quadrupolar nuclei; Structure determination; TROSY; Ultrahigh magnetic fields; Whole cell NMR.

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Figures

Fig. 1
Fig. 1
(a) Advancements in magnetic field strengths for NMR over the last few decades. Yellow indicates LTS magnets while green indicates dual LTS/HTS magnets. The dashed line indicates a frequency of 1 GHz (23.5 T). (b) General schematic of dual LTS/HTS magnet including shim coils and superconducting magnet coils. The precise number of LTS and HTS coils may vary. Purple represents superconducting shim coils, while blue represents outer NbTi LTS coils, orange represents Nb3Sn inner LTS coils, and green represents HTS coils. Within the magnet bore, maroon (outer) and pink (inner) bars represent the ferromagnetic and room temperature shim coils respectively.
Fig. 2
Fig. 2
(a) Simulated plots of TROSY15NH relaxation rates and relative peak heights as a function of magnetic field strength. (b) Pulse sequences for the1H- (right) and15N- (left) detected 2D TROSY-HSQC experiments. (c) Left:15N-detected TROSY-HSQC, right:1H-detected TROSY-HSQC. (d) Top:15N projection of the 2D15N-detected TROSY-HSQC (left) and1H-detected TROSY-HSQC (right). Bottom: Selected15N cross sections of the 2D15N-detected TROSY-HSQC (left) and1H-detected TROSY-HSQC (right). Reprinted with permission from Takeuchi, K et al.,J. Biomol. NMR.,2015,63 (4), 323–331. Copyright 2015 Springer.
Fig. 3
Fig. 3
(a) Pulse sequences of 3D (H)CCH and HCC(H) experiments for RAP-labeled proteins with (b) schematic of magnetization transfers at each step of the pulse sequence. Adapted with permission from Asami, S et al.,J. Biomol. NMR.,2012,52 (1), 31–39. Copyright 2012 Springer.
Fig. 4
Fig. 4
Paramagnetic effects in Cu2+/Co2+ loaded SOD by MAS NMR. (a)15N and13CO R1 and R1ρ relaxation rates for Cu+- (red, diamagnetic) and Cu2+- (blue, paramagnetic) bound SOD (144). (b) CP-HSQC spectra of Zn2+- (black, diamagnetic) and Co2+- (purple, paramagnetic) bound SOD (144). (c) Left: anisotropic susceptibility tensor for Co2+ with respect to SOD structure. Right: Identification and assignment of PCS from 3D (H)CONH experiment, color scheme as in (b). (d) Expansions of select PCSs from 3D (H)CONH experiment, color scheme as in (b). (e-h) Structure refinement of SOD (143). (e) No paramagnetic restraints, (f) with PRE restraints, (g) with PCS restraints, (h) with PRE and PCS restraints. (a) Reprinted with permission from Knight, MJ et al.,Proc. Nat. Acad. Sci.,2012,46 (9), 2108–2116. (b-d) Reprinted with permission from Knight, MJ et al.,J. Am. Chem. Soc.,2012,134 (36), 14730–14733. Copyright 2012 American Chemical Society. (e-h) Reprinted with permission from Knight, MJ et al.,Acc. Chem. Res.,2013,46 (9), 2108–2116. Copyright 2013 American Chemical Society.
Fig. 5
Fig. 5
Structure determination of the viral protein AP205CP assemblies by MAS NMR at ultrahigh field. (a) (left) A superposition of15N-1H CP-HSQC spectra of (red) a fully protonated sample at 100 kHz and (black) a perdeuterated, 100% NH sample at 60 kHz MAS frequency. (right) Expansions of13C-1H CP-HSQC spectra of AP205CP methyl (top) and Hα-Cα (bottom) regions at 100 kHz MAS and 1 GHz field. (b)13C-13C correlation spectrum (top) and select strips of a 3D (H)CCH spectrum of AP205CP (bottom). (c) Selected strips of a 3D (H)CHH spectrum for determination of distance restraints. The intermolecular peaks are underlined. (d) Expansion of the AP205CP dimer structure showing the restraints extracted from (c). Adapted with permission from Andreas, LB et al.,Proc. Nat. Acad. Sci.,2016,113 (33), 9187–9192.
Fig. 6
Fig. 6
Structural and mechanistic studies of the membrane protein Influenza A M2 by MAS NMR at ultrahigh field. (a) Assigned15N-1H CP-HSQC spectrum recorded at 60 kHz MAS and 1 GHz field. Peak doubling labeled in black and blue indicates the different conformations for each subunit of the dimer. (b) Methyl region of a 2D13C-1H J-based spectrum of13C,2H2,1H-ILV labeled M2 and (c-f) selected strips of a 4D HCHHCH spectrum. (g) H37’-W41 inter-residue cross peaks from an (H)NHHRFDR experiment. (h) Positions of H37 and W41 in the M2 dimer of dimers. (i) M2 pore surface indicating water accessibility/pore width: red: < 1 H2O, green = 1 H2O, and blue > 1 H2O. (j) C-terminal H37 and W41 adopts two different conformations in the dimer of dimers. Adapted with permission from Andreas, LB et al.,J. Am. Chem. Soc.,2015,137 (47), 14877–14886. Copyright 2015 American Chemical Society.
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