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Journal articles on the topic 'TROSY NMR'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 February 2022

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1

Pervushin, Konstantin. "Impact of Transverse Relaxation Optimized Spectroscopy (TROSY) on NMR as a technique in structural biology." Quarterly Reviews of Biophysics 33, no. 2 (2000): 161–97. http://dx.doi.org/10.1017/s0033583500003619.

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1. Transverse relaxation and the molecular size limit in liquid state NMR 1612. TROSY: how does it work? 1632.1 Transverse relaxation in coupled spin systems 1632.2 The TROSY effect, relaxation due to remote protons and 2H isotope labeling 1653. Direct heteronuclear chemical shift correlations 1683.1 Single-Quantum [15N,1H]-TROSY 1683.2 Zero-Quantum [15N,1H]-TROSY 1713.3 Single-Quantum TROSY with aromatic 13C–1H moieties 1764. Resonance assignment and NOE spectroscopy of large biomolecules 1804.1 TROSY-based triple resonance experiments for 13C, 15N and 1HN backbone resonance assignment in uni
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2

Pervushin, Konstantin, Beat Vögeli, and Alexander Eletsky. "Longitudinal1H Relaxation Optimization in TROSY NMR Spectroscopy." Journal of the American Chemical Society 124, no. 43 (2002): 12898–902. http://dx.doi.org/10.1021/ja027149q.

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3

Chevelkov, Veniamin, and Bernd Reif. "TROSY effects in MAS solid-state NMR." Concepts in Magnetic Resonance Part A 32A, no. 2 (2008): 143–56. http://dx.doi.org/10.1002/cmr.a.20106.

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4

Xia, Youlin, Kong Hung Sze, Ning Li, Pang Chui Shaw, and Guang Zhu. "Protein Dynamics Measurements by 3D HNCO Based NMR Experiments." Spectroscopy 16, no. 1 (2002): 1–13. http://dx.doi.org/10.1155/2002/828353.

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Protein dynamics can be characterized by relaxation parameters obtained from traditional 2D HSQC based NMR experiments. This approach is hampered when applied to proteins with severe spectral overlap. In the present work, several novel 3D TROSY-HNCO and 3D HSQC-HNCO based NMR experiments were applied for measuring15NT1,T2and1H-15N NOE with improved spectral dispersion by introducing a third13C dimension. The number of phase cycling steps in these 3D pulse sequences was restricted to two in order to minimize the time required to perform the dynamics measurements. For a uniformly 100%15N, 100%13
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5

Zhu, Guang, and Xuejun Yao. "TROSY-based NMR experiments for NMR studies of large biomolecules." Progress in Nuclear Magnetic Resonance Spectroscopy 52, no. 1 (2008): 49–68. http://dx.doi.org/10.1016/j.pnmrs.2007.10.001.

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6

Luchinat, Enrico, Letizia Barbieri, Matteo Cremonini, and Lucia Banci. "Protein in-cell NMR spectroscopy at 1.2 GHz." Journal of Biomolecular NMR 75, no. 2-3 (2021): 97–107. http://dx.doi.org/10.1007/s10858-021-00358-w.

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AbstractIn-cell NMR spectroscopy provides precious structural and functional information on biological macromolecules in their native cellular environment at atomic resolution. However, the intrinsic low sensitivity of NMR imposes a big limitation in the applicability of the methodology. In this respect, the recently developed commercial 1.2 GHz NMR spectrometer is expected to introduce significant benefits. However, cell samples may suffer from detrimental effects at ultrahigh fields, that must be carefully evaluated. Here we show the first in-cell NMR spectra recorded at 1.2 GHz on human cel
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7

Maleckis, Ansis, Iresha D. Herath, and Gottfried Otting. "Synthesis of 13C/19F/2H labeled indoles for use as tryptophan precursors for protein NMR spectroscopy." Organic & Biomolecular Chemistry 19, no. 23 (2021): 5133–47. http://dx.doi.org/10.1039/d1ob00611h.

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Cell-free protein synthesis using <sup>19</sup>F–<sup>13</sup>C and <sup>1</sup>H–<sup>13</sup>C spin pair containing indoles as tryptophan precursors enables site-specific labeling of proteins for <sup>19</sup>F NMR and TROSY NMR studies.
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8

Robertson, Angus J., Jinfa Ying, and Ad Bax. "Four-dimensional NOE-NOE spectroscopy of SARS-CoV-2 Main Protease to facilitate resonance assignment and structural analysis." Magnetic Resonance 2, no. 1 (2021): 129–38. http://dx.doi.org/10.5194/mr-2-129-2021.

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Abstract. Resonance assignment and structural studies of larger proteins by nuclear magnetic resonance (NMR) can be challenging when exchange broadening, multiple stable conformations, and 1H back-exchange of the fully deuterated chain pose problems. These difficulties arise for the SARS-CoV-2 Main Protease, a homodimer of 2 × 306 residues. We demonstrate that the combination of four-dimensional (4D) TROSY-NOESY-TROSY spectroscopy and 4D NOESY-NOESY-TROSY spectroscopy provides an effective tool for delineating the 1H–1H dipolar relaxation network. In combination with detailed structural inform
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9

Maurer, Till. "TROSY und Co: NMR-Methoden für die Wirkstoffentwicklung." Nachrichten aus der Chemie 48, no. 11 (2000): 1336–41. http://dx.doi.org/10.1002/nadc.20000481107.

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10

Zhu, Guang, Youlin Xia, Linda K. Nicholson, and Kong Hung Sze. "Protein Dynamics Measurements by TROSY-Based NMR Experiments." Journal of Magnetic Resonance 143, no. 2 (2000): 423–26. http://dx.doi.org/10.1006/jmre.2000.2022.

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11

Klein, Brittney A., and Brian D. Sykes. "Feasibility of trifluoromethyl TROSY NMR at high magnetic fields." Journal of Biomolecular NMR 73, no. 10-11 (2019): 519–23. http://dx.doi.org/10.1007/s10858-019-00266-0.

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12

Kitevski-LeBlanc, Julianne L., Tairan Yuwen, Pamela N. Dyer, Johannes Rudolph, Karolin Luger, and Lewis E. Kay. "Investigating the Dynamics of Destabilized Nucleosomes Using Methyl-TROSY NMR." Journal of the American Chemical Society 140, no. 14 (2018): 4774–77. http://dx.doi.org/10.1021/jacs.8b00931.

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13

Rosenzweig, Rina, and Lewis E. Kay. "Bringing Dynamic Molecular Machines into Focus by Methyl-TROSY NMR." Annual Review of Biochemistry 83, no. 1 (2014): 291–315. http://dx.doi.org/10.1146/annurev-biochem-060713-035829.

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14

Loria, J. Patrick, Mark Rance, and Arthur G. Palmer. "Transverse-Relaxation-Optimized (TROSY) Gradient-Enhanced Triple-Resonance NMR Spectroscopy." Journal of Magnetic Resonance 141, no. 1 (1999): 180–84. http://dx.doi.org/10.1006/jmre.1999.1891.

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15

Ritter, Christiane, Thorsten Lührs, Witek Kwiatkowski, and Roland Riek. "3d Trosy-HncaCodedcb and Trosy-HncaCodedco Experiments: Triple Resonance nmr Experiments With two Sequential Connectivity Pathways and High Sensitivity." Journal of Biomolecular NMR 28, no. 3 (2004): 289–94. http://dx.doi.org/10.1023/b:jnmr.0000013698.89582.dc.

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16

Tugarinov, Vitali, Remco Sprangers, and Lewis E. Kay. "Line Narrowing in Methyl-TROSY Using Zero-Quantum1H-13C NMR Spectroscopy." Journal of the American Chemical Society 126, no. 15 (2004): 4921–25. http://dx.doi.org/10.1021/ja039732s.

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17

Weigelt, Johan. "Single Scan, Sensitivity- and Gradient-Enhanced TROSY for Multidimensional NMR Experiments." Journal of the American Chemical Society 120, no. 41 (1998): 10778–79. http://dx.doi.org/10.1021/ja982649y.

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18

Abramov, Gili, Algirdas Velyvis, Enrico Rennella, Leo E. Wong, and Lewis E. Kay. "A methyl-TROSY approach for NMR studies of high-molecular-weight DNA with application to the nucleosome core particle." Proceedings of the National Academy of Sciences 117, no. 23 (2020): 12836–46. http://dx.doi.org/10.1073/pnas.2004317117.

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The development of methyl-transverse relaxation-optimized spectroscopy (methyl-TROSY)–based NMR methods, in concert with robust strategies for incorporation of methyl-group probes of structure and dynamics into the protein of interest, has facilitated quantitative studies of high-molecular-weight protein complexes. Here we develop a one-pot in vitro reaction for producing NMR quantities of methyl-labeled DNA at the C5 and N6 positions of cytosine (5mC) and adenine (6mA) nucleobases, respectively, enabling the study of high-molecular-weight DNA molecules using TROSY approaches originally develo
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19

Sprangers, Remco, Xiaoming Li, Xinliang Mao, John L. Rubinstein, Aaron D. Schimmer, and Lewis E. Kay. "TROSY-Based NMR Evidence for a Novel Class of 20S Proteasome Inhibitors†." Biochemistry 47, no. 26 (2008): 6727–34. http://dx.doi.org/10.1021/bi8005913.

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20

Riek, Roland, Konstantin Pervushin, and Kurt Wüthrich. "TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution." Trends in Biochemical Sciences 25, no. 10 (2000): 462–68. http://dx.doi.org/10.1016/s0968-0004(00)01665-0.

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21

Schütz, Stefan, and Remco Sprangers. "Methyl TROSY spectroscopy: A versatile NMR approach to study challenging biological systems." Progress in Nuclear Magnetic Resonance Spectroscopy 116 (February 2020): 56–84. http://dx.doi.org/10.1016/j.pnmrs.2019.09.004.

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22

Salzmann, Michael, Gerhard Wider, Konstantin Pervushin, Hans Senn, and Kurt Wüthrich. "TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins." Journal of the American Chemical Society 121, no. 4 (1999): 844–48. http://dx.doi.org/10.1021/ja9834226.

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23

Religa, T. L., R. Sprangers, and L. E. Kay. "Dynamic Regulation of Archaeal Proteasome Gate Opening As Studied by TROSY NMR." Science 328, no. 5974 (2010): 98–102. http://dx.doi.org/10.1126/science.1184991.

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24

Toyama, Yuki, Robert W. Harkness, Tim Y. T. Lee, Jason T. Maynes, and Lewis E. Kay. "Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR." Proceedings of the National Academy of Sciences 118, no. 11 (2021): e2025022118. http://dx.doi.org/10.1073/pnas.2025022118.

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Human High temperature requirement A2 (HtrA2) is a mitochondrial protease chaperone that plays an important role in cellular proteostasis and in regulating cell-signaling events, with aberrant HtrA2 function leading to neurodegeneration and parkinsonian phenotypes. Structural studies of the enzyme have established a trimeric architecture, comprising three identical protomers in which the active sites of each protease domain are sequestered to form a catalytically inactive complex. The mechanism by which enzyme function is regulated is not well understood. Using methyl transverse relaxation opt
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25

Burz, David, Leonard Breindel, and Alexander Shekhtman. "The Inescapable Effects of Ribosomes on In-Cell NMR Spectroscopy and the Implications for Regulation of Biological Activity." International Journal of Molecular Sciences 20, no. 6 (2019): 1297. http://dx.doi.org/10.3390/ijms20061297.

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The effects of RNA on in-cell NMR spectroscopy and ribosomes on the kinetic activity of several metabolic enzymes are reviewed. Quinary interactions between labelled target proteins and RNA broaden in-cell NMR spectra yielding apparent megadalton molecular weights in-cell. The in-cell spectra can be resolved by using cross relaxation-induced polarization transfer (CRINEPT), heteronuclear multiple quantum coherence (HMQC), transverse relaxation-optimized, NMR spectroscopy (TROSY). The effect is reproduced in vitro by using reconstituted total cellular RNA and purified ribosome preparations. Fur
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26

Kay, Lewis E. "Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view." Journal of Magnetic Resonance 210, no. 2 (2011): 159–70. http://dx.doi.org/10.1016/j.jmr.2011.03.008.

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27

FERNANDEZ, C. "TROSY in NMR studies of the structure and function of large biological macromolecules." Current Opinion in Structural Biology 13, no. 5 (2003): 570–80. http://dx.doi.org/10.1016/j.sbi.2003.09.009.

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28

Morgan, William D., Thomas A. Frenkiel, Matthew J. Lock, Munira Grainger, and Anthony A. Holder. "Precise Epitope Mapping of Malaria Parasite Inhibitory Antibodies by TROSY NMR Cross-Saturation†." Biochemistry 44, no. 2 (2005): 518–23. http://dx.doi.org/10.1021/bi0482957.

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29

Yang, Daiwen, and Lewis E. Kay. "TROSY Triple-Resonance Four-Dimensional NMR Spectroscopy of a 46 ns Tumbling Protein." Journal of the American Chemical Society 121, no. 11 (1999): 2571–75. http://dx.doi.org/10.1021/ja984056t.

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30

OKADA, Akihiko. "Polymer Characterization Using Two-Dimensional Nuclear Magnetic Resonance (2D-NMR) — Application of TROSY." KOBUNSHI RONBUNSHU 69, no. 5 (2012): 242–45. http://dx.doi.org/10.1295/koron.69.242.

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31

Mulry, Emma, Arka Prabha Ray, and Matthew T. Eddy. "Production of a Human Histamine Receptor for NMR Spectroscopy in Aqueous Solutions." Biomolecules 11, no. 5 (2021): 632. http://dx.doi.org/10.3390/biom11050632.

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G protein-coupled receptors (GPCRs) bind a broad array of extracellular molecules and transmit intracellular signals that initiate physiological responses. The signal transduction functions of GPCRs are inherently related to their structural plasticity, which can be experimentally observed by spectroscopic techniques. Nuclear magnetic resonance (NMR) spectroscopy in particular is an especially advantageous method to study the dynamic behavior of GPCRs. The success of NMR studies critically relies on the production of functional GPCRs containing stable-isotope labeled probes, which remains a ch
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32

Frickel, E. M., R. Riek, I. Jelesarov, A. Helenius, K. Wuthrich, and L. Ellgaard. "TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain." Proceedings of the National Academy of Sciences 99, no. 4 (2002): 1954–59. http://dx.doi.org/10.1073/pnas.042699099.

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33

Salzmann, M., K. Pervushin, G. Wider, H. Senn, and K. Wuthrich. "TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins." Proceedings of the National Academy of Sciences 95, no. 23 (1998): 13585–90. http://dx.doi.org/10.1073/pnas.95.23.13585.

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34

Pervushin, K. V., G. Wider, R. Riek, and K. Wuthrich. "The 3D NOESY-[1H,15N,1H]-ZQ-TROSY NMR experiment with diagonal peak suppression." Proceedings of the National Academy of Sciences 96, no. 17 (1999): 9607–12. http://dx.doi.org/10.1073/pnas.96.17.9607.

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35

Frueh, Dominique P., Zhen-Yu J. Sun, David A. Vosburg, Christopher T. Walsh, Jeffrey C. Hoch, and Gerhard Wagner. "Non-uniformly Sampled Double-TROSY hNcaNH Experiments for NMR Sequential Assignments of Large Proteins." Journal of the American Chemical Society 128, no. 17 (2006): 5757–63. http://dx.doi.org/10.1021/ja0584222.

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36

Clark, Lindsay, Jacob A. Zahm, Rustam Ali, et al. "Methyl labeling and TROSY NMR spectroscopy of proteins expressed in the eukaryote Pichia pastoris." Journal of Biomolecular NMR 62, no. 3 (2015): 239–45. http://dx.doi.org/10.1007/s10858-015-9939-2.

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37

Takeuchi, Koh, Haribabu Arthanari, Ichio Shimada, and Gerhard Wagner. "Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR." Journal of Biomolecular NMR 63, no. 4 (2015): 323–31. http://dx.doi.org/10.1007/s10858-015-9991-y.

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38

Hao, Zhan-Xi, Min Tan, Chang-Dong Liu, Rui Feng, En-Duo Wang, and Guang Zhu. "Studying base pair open-close kinetics of tRNALeuby TROSY-based proton exchange NMR spectroscopy." FEBS Letters 584, no. 21 (2010): 4449–52. http://dx.doi.org/10.1016/j.febslet.2010.10.002.

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39

Miyanoiri, Yohei, Mitsuhiro Takeda, Tsutomu Terauchi, and Masatsune Kainosho. "Recent developments in isotope-aided NMR methods for supramolecular protein complexes –SAIL aromatic TROSY." Biochimica et Biophysica Acta (BBA) - General Subjects 1864, no. 2 (2020): 129439. http://dx.doi.org/10.1016/j.bbagen.2019.129439.

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40

Whitaker, Amy M., Mandar T. Naik, and Gregory D. Reinhart. "Propogation of the Allosteric Signal in Bacillus Stearothermophilus Phosphofructokinase Examined by Methyl-TROSY NMR." Biophysical Journal 108, no. 2 (2015): 30a—31a. http://dx.doi.org/10.1016/j.bpj.2014.11.191.

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41

Meissner, Axel, and Ole Winneche Sørensen. "The Role of Coherence Transfer Efficiency in Design of TROSY-Type Multidimensional NMR Experiments." Journal of Magnetic Resonance 139, no. 2 (1999): 439–42. http://dx.doi.org/10.1006/jmre.1999.1788.

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42

Meissner, Axel, and Ole Winneche Sørensen. "Suppression of Diagonal Peaks in Three-Dimensional Protein NMR TROSY-Type HCCH Correlation Experiments." Journal of Magnetic Resonance 144, no. 1 (2000): 171–74. http://dx.doi.org/10.1006/jmre.2000.2046.

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43

Huang, Rui, Zev A. Ripstein, Rafal Augustyniak, et al. "Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study." Proceedings of the National Academy of Sciences 113, no. 29 (2016): E4190—E4199. http://dx.doi.org/10.1073/pnas.1603980113.

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The AAA+ (ATPases associated with a variety of cellular activities) enzymes play critical roles in a variety of homeostatic processes in all kingdoms of life. Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), the archaeal homolog of the ubiquitous AAA+ protein Cdc48/p97, functions in concert with the 20S proteasome by unfolding substrates and passing them on for degradation. Here, we present electron cryomicroscopy (cryo-EM) maps showing that VAT undergoes large conformational rearrangements during its ATP hydrolysis cycle that differ dramatically from the conformationa
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44

Pervushin, Konstantin, Roland Riek, Gerhard Wider, and Kurt Wüthrich. "Transverse Relaxation-Optimized Spectroscopy (TROSY) for NMR Studies of Aromatic Spin Systems in13C-Labeled Proteins." Journal of the American Chemical Society 120, no. 25 (1998): 6394–400. http://dx.doi.org/10.1021/ja980742g.

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45

Liu, Aizhuo, Yue Li, Lishan Yao, and Honggao Yan. "Simultaneous NMR assignment of backbone and side chain amides in large proteins with IS-TROSY." Journal of Biomolecular NMR 36, no. 4 (2006): 205–14. http://dx.doi.org/10.1007/s10858-006-9072-3.

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46

Meissner, Axel, and Ole Winneche Sørensen. "Suppression of Diagonal Peaks in TROSY-Type 1H NMR NOESY Spectra of 15N-Labeled Proteins." Journal of Magnetic Resonance 140, no. 2 (1999): 499–503. http://dx.doi.org/10.1006/jmre.1999.1860.

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47

Siemons, Lucas, Harold W. Mackenzie, Vaibhav Kumar Shukla, and D. Flemming Hansen. "Intra-residue methyl–methyl correlations for valine and leucine residues in large proteins from a 3D-HMBC-HMQC experiment." Journal of Biomolecular NMR 73, no. 12 (2019): 749–57. http://dx.doi.org/10.1007/s10858-019-00287-9.

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Abstract Methyl-TROSY based NMR experiments have over the last two decades become one of the most important means to characterise dynamics and functional mechanisms of large proteins and macromolecular machines in solution. The chemical shift assignment of methyl groups in large proteins is, however, still not trivial and it is typically performed using backbone-dependent experiments in a ‘divide and conquer’ approach, mutations, structure-based assignments or a combination of these. Structure-based assignment of methyl groups is an emerging strategy, which reduces the time and cost required a
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48

Morgan, William D., Matthew J. Lock, Thomas A. Frenkiel, Munira Grainger, and Anthony A. Holder. "Malaria parasite-inhibitory antibody epitopes on Plasmodium falciparum merozoite surface protein-119 mapped by TROSY NMR." Molecular and Biochemical Parasitology 138, no. 1 (2004): 29–36. http://dx.doi.org/10.1016/j.molbiopara.2004.06.014.

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49

Guo, Chenyun, Daoning Zhang, and Vitali Tugarinov. "An NMR Experiment for Simultaneous TROSY-Based Detection of Amide and Methyl Groups in Large Proteins." Journal of the American Chemical Society 130, no. 33 (2008): 10872–73. http://dx.doi.org/10.1021/ja8036178.

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50

Rudiger, S., S. M. V. Freund, D. B. Veprintsev, and A. R. Fersht. "CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90." Proceedings of the National Academy of Sciences 99, no. 17 (2002): 11085–90. http://dx.doi.org/10.1073/pnas.132393699.

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