Ahlawat S, Mote KR, Lakomek NA, Agarwal V (2022) Solid-state NMR - methods for biological solids. Chem Rev 122(10):9643–9737. https://doi.org/10.1021/acs.chemrev.1c00852
Ahlawat S, Mopidevi SMV, Taware PP, Raran-Kurussi S, Mote KR, Agarwal V (2023) Assignment of aromatic side-chain spins and characterization of their distance restraints at fast MAS. J Struct Biol X 7(100):082. https://doi.org/10.1016/j.yjsbx.2022.100082
Andreas LB, Jaudzems K, Stanek J, Lalli D, Bertarello A, Le Marchand T, Cala-De Paepe D, Kotelovica S, Akopjana I, Knott B, Wegner S, Engelke F, Lesage A, Emsley L, Tars K, Herrmann T, Pintacuda G (2016) Structure of fully protonated proteins by proton-detected magic-angle spinning NMR. Proc Natl Acad Sci U S A 113(33):9187–9192. https://doi.org/10.1073/pnas.1602248113
Bak M, Rasmussen JT, Nielsen NC (2000) SIMPSON: a general simulation program for solid-state NMR spectroscopy. J Magn Reson 147(2):296–330. https://doi.org/10.1016/j.jmr.2011.09.008
Bayro MJ, Chen B, Yau WM, Tycko R (2014) Site-specific structural variations accompanying tubular assembly of the HIV-1 capsid protein. J Mol Biol 426(5):1109–1127. https://doi.org/10.1016/j.jmb.2013.12.021
Bellstedt P, Seiboth T, Häfner S, Kutscha H, Ramachandran R, Görlach M (2013) Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete nmr data sets. J Biomol NMR 57(1):65–72. https://doi.org/10.1007/s10858-013-9768-0
Fraga H, Arnaud CA, Gauto DF, Audin M, Kurauskas V, Macek P, Krichel C, Guan JY, Boisbouvier J, Sprangers R et al (2017) Solid-state NMR H-N-(c)-H and H-N-C-C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem 18(19):2697–2703. https://doi.org/10.1002/cphc.201700572
Franks WT, Zhou DH, Wylie BJ, Money BG, Graesser DT, Frericks HL, Sahota G, Rienstra CM (2005) Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): <inlineGraphic />N and <inlineGraphic />C chemical shift assignments and conformational analysis. J Am Chem Soc 127(35):12,291-12,305. https://doi.org/10.1021/ja044497e
Ghosh M, Rienstra CM (2017) \(^1\)H-detected REDOR with fast magic-angle spinning of a deuterated protein. J Phys Chem B 121(36):8503–8511. https://doi.org/10.1021/acs.jpcb.7b07313
Gullion T, Pennington CH (1998) \(\theta\)-REDOR - an MAS NMR method to simplify multiple coupled heteronuclear spin systems. Chem Phys Lett 290:88–93
Gullion T, Schaefer J (1989) Rotational-echo double-resonance NMR. J Magn Reson 81(1):196–200. https://doi.org/10.1016/0022-2364(89)90280-1
Haller JD, Schanda P (2013) Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: A critical evaluation of experimental approaches and application to crystalline ubiquitin. J Biomol NMR 57(3):263–280. https://doi.org/10.1007/s10858-013-9787-x
Helmus JJ, Jaroniec CP (2013) Nmrglue: An open source Python package for the analysis of multidimensional NMR data. J Biomol NMR 55(4):355–367. https://doi.org/10.1007/s10858-013-9718-x
Hing AW, Vega S, Schaefer J (1992) Transferred-echo double-resonance NMR. J Magn Reson 96(1):205–209. https://doi.org/10.1016/0022-2364(92)90305-Q
Hirschinger J (2008) Analytical solutions to several magic-angle spinning NMR experiments. Solid State Nucl Magn Reson 34:210–233
Hong M (2000) Solid-state NMR determination of \(^\)C\(\alpha\) chemical shift anisotropies for the identification of protein secondary structure. J Am Chem Soc 122(15):3762–3770
Hu KN, Qiang W, Bermejo GA, Schwieters CD, Tycko R (2012) Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide \(^\)N–\(^\)N and carbonyl \(^\)C–\(^\)C dipolar recoupling data. J Magn Reson 218:115–127. https://doi.org/10.1016/j.jmr.2012.03.001
Huster D, Yamaguchi S, Hong M (2000) Efficient <inlineGraphic />-sheet identification in proteins by solid-state NMR spectroscopy. J Am Chem Soc 122(46):11,320-11,327. https://doi.org/10.1021/ja001674c
Jain MG, Mote KR, Hellwagner J, Rajalakshmi G, Ernst M, Madhu PK, Agarwal V (2019) Measuring strong one-bond dipolar couplings using REDOR in magic-angle spinning solid-state NMR. J Chem Phys 150(13):134,201. https://doi.org/10.1063/1.5088100
Jain MG, Rajalakshmi G, Madhu PK, Agarwal V, Mote KR (2020) Overcoming prohibitively large radiofrequency demands for the measurement of internuclear distances with solid-state NMR under fast magic-angle spinning. J Phys Chem B 124(8):1444–1451. https://doi.org/10.1021/acs.jpcb.9b11849
Jaroniec CP, Filip C, Griffin RG (2002) 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly <inlineGraphic />, <inlineGraphic />-labeled solids. J Am Chem Soc 124(36):10,728-10,742. https://doi.org/10.1021/ja026385y
Lacabanne D, Meier BH, Böckmann A (2017) Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy. J Biomol NMR 0123456789. https://doi.org/10.1007/s10858-017-0156-z
Lee W, Rahimi M, Lee Y, Chiu A (2021) POKY: a software suite for multidimensional NMR and 3d structure calculation of biomolecules. Bioinformatics 37(18):3041–3042. https://doi.org/10.1093/bioinformatics/btab180
Lewandowski JR, Dumez JN, Akbey U, Lange S, Emsley L, Oschkinat H (2011) Enhanced resolution and coherence lifetimes in the solid-state NMR spectroscopy of perdeuterated proteins under ultrafast magic-angle spinning. J Phys Chem Lett 2(17):2205–2211, 10/bc58wq
Liivak O, Zax DB (2000) Multiple simultaneous distance determinations: Application of rotational echo double resonance nuclear magnetic resonance to \(IS_2\) spin networks. J Chem Phys 113(3):1088–1096. https://doi.org/10.1063/1.481887
Liivak O, Zax DB (2001) Rotational echo double resonance in \(is_n\) spin networks: Deconvolution of multiple dipole–dipole couplings. J Chem Phys 115(1):402–409. https://doi.org/10.1063/1.1378040
Lin MT, Sperling LJ, Frericks Schmidt HL, Tang M, Samoilova RI, Kumasaka T, Iwasaki T, Sa D, Rienstra CM, Gennis RB (2011) A rapid and robust method for selective isotope labeling of proteins. Methods 55(4):370–378. https://doi.org/10.1016/j.ymeth.2011.08.019
Lu JX, Qiang W, Yau WM, Schwieters CD, Meredith SC, Tycko R (2013) Molecular structure of \(\beta\)-amyloid fibrils in alzheimer’s disease brain tissue. Cell 154(6):1257–68, 10/gfj8cr
Maciejewski MW, Schuyler AD, Gryk MR, Moraru II, Romero PR, Ulrich EL, Eghbalnia HR, Livny M, Delaglio F, Hoch JC (2017) NMRbox: A resource for biomolecular NMR computation. Biophys J 112(8):1529–1534. https://doi.org/10.1016/j.bpj.2017.03.011
Marchand TL, Schubeis T, Bonaccorsi M, Paluch P, Lalli D, Pell AJ, Andreas LB, Jaudzems K, Stanek J, Pintacuda G (2022) \(^ \text\)-detected biomolecular NMR under fast magic-angle spinning. Chem Rev 122(10):9943–10,018. https://doi.org/10.1021/acs.chemrev.1c00918
Murray DT, Kato M, Lin Y, Thurber KR, Hung I, McKnight SL, Tycko R (2017) Structure of FUS protein fibrils and its relevance to self-assembly and phase separation of low-complexity domains. Cell https://doi.org/10.1016/j.cell.2017.08.048
Nowakowski M, Saxena S, Stanek J, Zerko S, Kozminski W (2015) Applications of high dimensionality experiments to biomolecular NMR. Prog Nucl Magn Reson Spectrosc 90–91:49–73. https://doi.org/10.1016/j.pnmrs.2015.07.001
Paravastu AK, Tycko R (2006) Frequency-selective homonuclear dipolar recoupling in solid state NMR. J Chem Phys. https://doi.org/10.1063/1.2192516
Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213–223. https://doi.org/10.1007/s10858-009-9333-z
Somberg NH, Sučec I, Hong M (2025) Assignment-free determination of ligand binding sites in proteins by solid-state nmr. J Am Chem Soc 147(30):26,534-26,545. https://doi.org/10.1021/jacs.5c06493
Taware PP, Jain MG, Raran-Kurussi S, Agarwal V, Madhu PK, Mote KR (2023) Measuring dipolar order parameters in nondeuterated proteins using solid-state NMR at the magic-angle-spinning frequency of 100 kHz. J Phys Chem Lett 14:3627–3635. https://doi.org/10.1021/acs.jpclett.3c00492
Tošner Z, Andersen R, Stevensson B, Edén M, Nielsen NC, Vosegaard T (2014) Computer-intensive simulation of solid-state NMR experiments using SIMPSON. J Magn Reson 246:79–93. https://doi.org/10.1016/j.jmr.2014.07.002
Tycko R (2007) Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR. J Chem Phys.
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