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Journal articles on the topic 'NMR structural analysis'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

Baek, Mihwa, Masakatsu Kamiya, Taichi Nakazumi, Satoshi Tomisawa, Yasuhiro Kumaki, Takashi Kikukawa, Makoto Demura, Keiichi Kawano, and Tomoyasu Aizawa. "3P011 Structural analysis of antimicrobial peptide CP1 with LPS by NMR(01A. Protein: Structure,Poster)." Seibutsu Butsuri 53, supplement1-2 (2013): S213. http://dx.doi.org/10.2142/biophys.53.s213_5.

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2

Marek, Radex, and Antonin Lycka. "15N NMR Spectroscopy in Structural Analysis." Current Organic Chemistry 6, no. 1 (January 1, 2002): 35–66. http://dx.doi.org/10.2174/1385272023374643.

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3

Muschin, Tegshi, and Takashi Yoshida. "Structural analysis of galactomannans by NMR spectroscopy." Carbohydrate Polymers 87, no. 3 (February 2012): 1893–98. http://dx.doi.org/10.1016/j.carbpol.2011.08.059.

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4

Tanaka, T. "NMR Structural Analysis of Escherichia coli Osmosensor EnvZ." Seibutsu Butsuri 40, supplement (2000): S111. http://dx.doi.org/10.2142/biophys.40.s111_3.

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5

TANAKA, Toshiyuki, and Mitsuhiko IKURA. "Structural Analysis of Proteins by Multi-Dimensional NMR." Journal of Synthetic Organic Chemistry, Japan 51, no. 6 (1993): 491–501. http://dx.doi.org/10.5059/yukigoseikyokaishi.51.491.

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6

Bechinger, Burkhard, Rudolf Kinder, Michael Helmle, Titus C. B. Vogt, Ulrike Harzer, and Susan Schinzel. "Peptide structural analysis by solid-state NMR spectroscopy." Biopolymers 51, no. 3 (1999): 174–90. http://dx.doi.org/10.1002/(sici)1097-0282(1999)51:3<174::aid-bip2>3.0.co;2-7.

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7

Marek, Radek, and Antonin Lycka. "ChemInform Abstract: 15N NMR Spectroscopy in Structural Analysis." ChemInform 33, no. 31 (May 20, 2010): no. http://dx.doi.org/10.1002/chin.200231300.

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8

Heald, Sarah L., Luciano Mueller, and Peter W. Jeffs. "Structural analysis of teicoplanin A2 by 2d NMR." Journal of Magnetic Resonance (1969) 72, no. 1 (March 1987): 120–38. http://dx.doi.org/10.1016/0022-2364(87)90179-x.

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9

YAMANOBE, TAKESHI. "Structural Analysis of Polymers by Solid State NMR." Sen'i Gakkaishi 77, no. 2 (February 15, 2021): P—69—P—75. http://dx.doi.org/10.2115/fiber.77.p-69.

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10

Sönnichsen, Frank D., Peter L. Davies, and Brian D. Sykes. "NMR structural studies on antifreeze proteins." Biochemistry and Cell Biology 76, no. 2-3 (May 1, 1998): 284–93. http://dx.doi.org/10.1139/o98-052.

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Antifreeze proteins (AFPs) are a structurally diverse class of proteins that bind to ice and inhibit its growth in a noncolligative manner. This adsorption-inhibition mechanism operating at the ice surface results in a lowering of the (nonequilibrium) freezing point below the melting point. A lowering of ~1°C, which is sufficient to prevent fish from freezing in ice-laden seawater, requires millimolar AFP levels in the blood. The solubility of AFPs at these millimolar concentrations and the small size of the AFPs (typically 3-15 kDa) make them ideal subjects for NMR analysis. Although fish AFPs are naturally abundant, seasonal expression, restricted access to polar fishes, and difficulties in separating numerous similar isoforms have made protein expression the method of choice for producing AFPs for structural studies. Expression of recombinant AFPs has also facilitated NMR analysis by permitting isotopic labeling with 15N and 13C and has permitted mutations to be made to help with the interpretation of NMR data. NMR analysis has recently solved two AFP structures and provided valuable information about the disposition of ice-binding side chains in a third. The potential exists to solve other AFP structures, including the newly described insect AFPs, and to use solid-state NMR techniques to address fundamental questions about the nature of the interaction between AFPs and ice.Key words: NMR spectroscopy, antifreeze, ice-binding affinity, review.

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11

Stockman, Brian J., and John L. Markley. "NMR analysis of ligand binding." Current Opinion in Structural Biology 2, no. 1 (February 1992): 52–56. http://dx.doi.org/10.1016/0959-440x(92)90176-8.

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12

LeMaster, David M. "Deuterium labelling in NMR structural analysis of larger proteins." Quarterly Reviews of Biophysics 23, no. 2 (May 1990): 133–74. http://dx.doi.org/10.1017/s0033583500005527.

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In the last few years since the early NMR structural studies of small proteins such as glucagon (Braunet al.1983) andlacrepresser headpiece (Zuiderweget al.1984) the quality of the structure determinations have improved considerably. Of major importance has been the introduction of phase sensitive detection in the Tl dimension (Stateset al.1982; Marion & Wüthrich, 1983) which has allowed for absorption presentation of 2D data with the resulting enhancement in resolution, accuracy of coupling constant measurements and accuracy of peak volume integrations. Introduction of new pulse sequences, advances in instrumentation and further developments in the structure calculation algorithms have also helped improve the quality of NMR structural analyses of proteins.

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13

KANEHASHI, Koji, Moriaki HATAKEYAMA, Koji SAITO, and Tooru MATSUMIYA. "Structural Analysis of Slag Using Multinuclear Solid State NMR." Tetsu-to-Hagane 89, no. 10 (2003): 1031–37. http://dx.doi.org/10.2355/tetsutohagane1955.89.10_1031.

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14

Shashkov, Alexander S., Dmitry E. Tsvetkov, Alexey A. Grachev, Olda A. Lapchinskaia, Maia F. Lavrova-Balashova, Valerii I. Ponomarenko, Genrikh S. Katrukha, and Nikolay E. Nifantiev. "Structural Analysis of Antibiotic INA 9301 from Amycolatopsis Orientalis." Natural Product Communications 3, no. 10 (October 2008): 1934578X0800301. http://dx.doi.org/10.1177/1934578x0800301010.

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The dalbaheptide antibiotic INA 9301 was isolated from a culture of Amycolatopsis orientalis. By using a combination of mass spectrometry and NMR spectroscopy, INA 9301 was assessed as N,N-dimethylvancomycin. Detailed 13C NMR characteristics of INA9301 in D2O and DMSO- d 6 are presented, together with 2D 1H-1H ROESY and 1H-13C gHMBC data, which confirmed the configurations of the asymmetric centers and spatial conformational shape of the molecule in aqueous solution.

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15

Yanagishita, H., K. Fukushima, S. M. Kim, S. W. Kang, T. Fujiwara, and H. Akutsu. "The structural analysis of mastoparan-X by solid state NMR." Seibutsu Butsuri 39, supplement (1999): S102. http://dx.doi.org/10.2142/biophys.39.s102_2.

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16

van de Pas, Daniel J., Bernadette Nanayakkara, Ian D. Suckling, and Kirk M. Torr. "Comparison of hydrogenolysis with thioacidolysis for lignin structural analysis." Holzforschung 68, no. 2 (February 1, 2014): 151–55. http://dx.doi.org/10.1515/hf-2013-0075.

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Abstract Mild hydrogenolysis has been compared with thioacidolysis as a method for degrading lignins in situ and in isolated form before analysis by gas chromatography/mass spectrometry and quantitative 31P nuclear magnetic resonance (NMR) spectroscopy. Both degradation methods gave similar levels of β-aryl ether-linked phenylpropane units that were released as monomers. Degradation by hydrogenolysis generally gave lower levels of total phenylpropane units when analyzed by 31P NMR, especially in the case of lignins with high levels of condensed units. Overall, these results indicate that mild hydrogenolysis could offer an alternative to thioacidolysis for probing lignin structure.

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17

Kanehashi, Koji, Koji Saito, and Hisashi Sugisawa. "Structural Analysis of Boron Carbide Using 2D11B-MQMAS NMR." Chemistry Letters 29, no. 6 (June 2000): 588–89. http://dx.doi.org/10.1246/cl.2000.588.

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18

Samuel, Dharmaraj, Hong Cheng, Paul W. Riley, Peter N. Walsh, and Heinrich Roder. "NMR Structural Analysis of Factor XI Apple 4 Domain." Blood 104, no. 11 (November 16, 2004): 1735. http://dx.doi.org/10.1182/blood.v104.11.1735.1735.

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Abstract Blood coagulation is achieved by two closely coordinated mechanisms: i) the contact factor, or intrinsic, pathway initiated by assembly of coagulation proteins on negatively charged surfaces, and ii) the extrinsic pathway initiated by exposure of tissue factor at the site of vascular injury. Although factor XI (FXI), a 160 KDa homodimeric plasma coagulation protein, can be activated either by FXIIa (generated by the contact factor pathway) or by thrombin (generated by the extrinsic or tissue factor pathway), recent evidence suggests that its unique dimeric structure is required for FXI-activation by thrombin on the platelet surface, leading to the initiation of the intrinsic pathway that is required for normal hemostasis. Each FXI monomer consists of an N-terminal heavy chain and a C-terminal trypsin-like catalytic light chain. The heavy chain consists of four homologous subunits called apple domains (designated A1 to A4). The A2 and A3 domains of one monomeric subunit bind to FIX, whereas the A3 domain of the other monomeric subunit binds to platelets. The A4 domain, which shares high (25–38%) sequence identity with other Apple domains, facilitates FXI dimer formation through an intermolecular disulfide bond at Cys-321. In the present study the rA4 domain was cloned and purified to determine its three-dimensional structure. Multidimensional heteronuclear NMR experiments were carried out using C13, N15, H2 labeled samples. Chemical shifts of the C13, N15 and H1 resonance of all the residues were assigned. Assignment of NOE cross peaks between inter- and intra-subunit amino acids is in progress. Preliminary results indicate that the monomeric structure of the A4 domain consists of six anti-parallel β-strands and an α-helix, stabilized by three cystine cross links. The orientations of charged residues and hydrophobic patches on different sides of the molecule may play important roles in the dimerization process of FXI.

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19

NAKAMURA, Yoshinobu, Masayo NODA, Kazuki TAKAKURA, Syuji FUJII, and Yoshiaki URAHAMA. "Structural Analysis of Pressure-Sensitive Adhesive using Pulse NMR." Journal of The Adhesion Society of Japan 52, no. 8 (August 1, 2016): 236–43. http://dx.doi.org/10.11618/adhesion.52.236.

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20

Bains, Jasleen Kaur, Julius Blechar, Vanessa de Jesus, Nathalie Meiser, Heidi Zetzsche, Boris Fürtig, Harald Schwalbe, and Martin Hengesbach. "Combined smFRET and NMR analysis of riboswitch structural dynamics." Methods 153 (January 2019): 22–34. http://dx.doi.org/10.1016/j.ymeth.2018.10.004.

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21

Lundborg, Magnus, and Göran Widmalm. "Structural Analysis of Glycans by NMR Chemical Shift Prediction." Analytical Chemistry 83, no. 5 (March 2011): 1514–17. http://dx.doi.org/10.1021/ac1032534.

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22

Kim, Nak-Kyoon, Yun-Sik Nam, and Kang-Bong Lee. "NMR methods for structural analysis of RNA: a Review." Journal of the Korean Magnetic Resonance Society 18, no. 1 (June 20, 2014): 5–9. http://dx.doi.org/10.6564/jkmrs.2014.18.1.005.

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23

Peres, Ivone, Sandra Rocha, Maria do Carmo Pereira, Manuel Coelho, Maria Rangel, and Galya Ivanova. "NMR structural analysis of epigallocatechin gallate loaded polysaccharide nanoparticles." Carbohydrate Polymers 82, no. 3 (October 2010): 861–66. http://dx.doi.org/10.1016/j.carbpol.2010.06.007.

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24

Spencer, Leigh, Eric Coomes, Eric Ye, Victor Terskikh, Adam Ramzy, Venkataraman Thangadurai, and Gillian R. Goward. "Structural analysis of lanthanum-containing battery materials using 139La solid-state NMR." Canadian Journal of Chemistry 89, no. 9 (September 2011): 1105–17. http://dx.doi.org/10.1139/v11-049.

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139La solid-state NMR spectra, acquired at 21.1 and 11.7 T, have been used to evaluate the structural properties of the lithium ion battery materials, La32Li16Fe6.4O67 and Li3xLa2/3–xTiO3. In particular, atomic-level disorder in the second coordination sphere environment of lanthanum in these materials has been indicated by the observation of a distribution in the asymmetry parameters and the quadrupolar coupling constants derived from experimental NMR spectra, and supported by theoretical calculations. For comparison, 139La NMR has been obtained for the two model compounds La2O3 and LaNbO4, in which there is no atomic-level disorder. Quadrupolar coupling constants in the range of 17 to 59 MHz have been measured, and these values are supported by previous work as well as theoretical predictions performed in CASTEP. It has been shown that 139La NMR is a useful tool for the structural analysis of lithium ion battery materials, and when combined with 7Li MAS NMR and powder X-ray diffraction, can be used to determine the structure of complex solid-state electrolyte and electrode materials.

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25

ASAKURA, Tetsuo. "Structural Analysis of Polymers Based on the Origin of the NMR Chemical Shift." KOBUNSHI RONBUNSHU 72, no. 11 (2015): 653–60. http://dx.doi.org/10.1295/koron.2015-0049.

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26

Kashiwai, H., K. Sakai, K. Sakurai, M. Hoshino, and Y. Goto. "Structural analysis of thiol modified beta-lactoglobulin by using NMR." Seibutsu Butsuri 40, supplement (2000): S24. http://dx.doi.org/10.2142/biophys.40.s24_3.

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27

Balakshin, Mikhail Yu, Ewellyn A. Capanema, Ricardo B. Santos, Hou-min Chang, and Hasan Jameel. "Structural analysis of hardwood native lignins by quantitative 13C NMR spectroscopy." Holzforschung 70, no. 2 (February 1, 2016): 95–108. http://dx.doi.org/10.1515/hf-2014-0328.

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Abstract Milled wood lignins from alkaline pretreated wood with very low sugar content and a wide range of syringyl-to-guaiacyl (S/G) ratio between 1.2 and 3.0 were isolated from 12 industrially valuable hardwood (HW) species. The lignin preparations were investigated by means of a comprehensive 13C nuclear magnetic resonance (NMR) methodology to address the possibilities and limitations of this approach for HW native lignins and to estimate the structural variations within HW lignins. Good correlations were found for different independent methods for the quantification of major lignin moieties. The results were reliable at the C6 level and not only for relative comparison. The correlation was good between methoxyl group determinations by wet chemistry and those by 13C NMR spectroscopy. The limitations of the 13C NMR method were also pointed out. The differences in the S/G ratios can be large, but other structural deviations are less significant. Strong correlations between the S/G ratios and the amounts of other structural peculiarities could not be found by the 13C NMR approach. However, with increasing S/G ratios, the β-O-4 content showed increasing tendencies and the degree of condensation showed decreasing tendencies.

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28

Delepierre, Muriel, Ada Prochnicka-Chalufour, and Lourival D. Possani. "1H NMR structural analysis of novel potassium blocking toxins using a nano-NMR probe." Toxicon 36, no. 11 (November 1998): 1599–608. http://dx.doi.org/10.1016/s0041-0101(98)00152-4.

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29

Tanaka, Yasuyuki. "Recent Advances in Structural Characterization of Elastomers." Rubber Chemistry and Technology 64, no. 3 (July 1, 1991): 325–85. http://dx.doi.org/10.5254/1.3538561.

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Abstract One of the main targets of the structural characterization of elastomers so far has been the correlation of the polymerization conditions with the properties of the resulting polymers. The first step is the analysis of polymer structure, such as the chemical composition of copolymers, isomeric structure of diene polymers, degree of branching, extent of modification, functionality of end groups, amounts of abnormal groups, tacticity, and so on. Progress in nuclear magnetic resonance spectroscopy (NMR) makes possible the second step, which is the structural characterization of polymer chains, such as the sequence distribution of comonomer units in copolymer, isomeric units in diene polymers, configurational sequences in vinyl polymers, head and tail arrangement of monomer units. Recent development of FT-NMR spectroscopy, high-field spectroscopy from 300 MHz to 600 MHz at 1H-NMR, solid-state 13C-NMR, and two-dimensional NMR has facilitated a more detailed analysis of these structural features. The complexity of the structure of elastomers, which is derived from highly controlled copolymerization processes, leads to the widespread application of modern FT-NMR spectroscopy. It may reasonably be said that a fair number of structural problems in elastomers has been solved by NMR analysis. The high sensitivity of Fourier-transform infrared spectroscopy (FT-IR) has enabled one to determine trace structural changes in elastomers. Coupled on-line techniques such as gas-chromatography-mass-spectrometry combined with pyrolysis, liquid chromatography-NMR, and gel permeation chromatography-FT-IR will be powerful tools for the characterization of elastomers. Progress in analytical instruments has stimulated the development of high-performance elastomers, the synthesis of new speciality elastomers, and the elucidation of mechanisms for property enhancements. The use of modern instruments and a combination of ordinary methods of structural analysis have satisfied needs to some extent. However, a newer method of structural characterization is always desired in order to achieve higher orders of information. for example, the characterization of inhomogeneity along the polymer chain and between the polymer chains has become an important problem, especially in polymer blend systems. As to the former problem, spectroscopic methods provide only limited information. Although the NMR and FT-IR spectroscopies are very powerful tools for the analysis of short sequence distributions, it is difficult to characterize the distribution of long sequences and hybrid systems containing random and blocked sequences along the polymer chain. Gel permeation chromatography (GPC) is one of the most popular techniques for the analysis of molecular-weight distribution. However, it provides complicated information including molecular-weight distribution and chemical-composition distribution in the case of copolymers. Recent progress of high-performance liquid chromatography (HPLC) has provided a new powerful tool for the structural characterization of copolymers. It is appropriate to review the recent advances in structural characterization of elastomers, especially the characterization of microstructure of polymer chains, from the viewpoints of methodology and applicability of new methods. As to the NMR analysis of elastomers, reviews are available. Here, considerable attention is focused on the procedures for the assignment of signals, because the applicability of a NMR method is based on the reliability of the signal assignments. The other topics are selected to provide direct information for polymer synthesis or polymer properties.

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30

TOHMURA, Shin-ichiro. "Structural Analysis of Cured Wood Adhesives Using Solid-State NMR." Journal of The Adhesion Society of Japan 48, no. 11 (2011): 381–88. http://dx.doi.org/10.11618/adhesion.48.381.

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31

Hoch, Jeffrey C., Christina Redfield, and Alan S. Stern. "Computer-aided analysis of protein NMR spectra." Current Opinion in Structural Biology 1, no. 6 (December 1991): 1036–41. http://dx.doi.org/10.1016/0959-440x(91)90103-z.

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32

Omichi, H., Y. Todokoro, K. Wakamatsu, T. Fujiwara, and H. Akutsu. "2P019 Structural analysis of G protein by solid state NMR." Seibutsu Butsuri 44, supplement (2004): S114. http://dx.doi.org/10.2142/biophys.44.s114_3.

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33

Fujiwara, T. "3SA56 Structural analysis of membrane protein by solid-state NMR." Seibutsu Butsuri 44, supplement (2004): S26. http://dx.doi.org/10.2142/biophys.44.s26_1.

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34

Lu, Rong, Kazuyuki Hattori, Zuyong Xia, Takashi Yoshida, Jianhong Yang, Lina Zhang, Yumin Du, Tetsuo Miyakoshi, and Toshiyuki Uryu. "Structural Analysis of Polysaccharides in Chinese Lacquer by NMR Spectroscopy." Sen'i Gakkaishi 55, no. 2 (1999): 47–56. http://dx.doi.org/10.2115/fiber.55.47.

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35

Marek, Radek, Antonin Lycka, Erkki Kolehmainen, Elina Sievanen, and Jaromir Tousek. "15N NMR Spectroscopy in Structural Analysis: An Update (2001 - 2005)." Current Organic Chemistry 11, no. 13 (September 1, 2007): 1154–205. http://dx.doi.org/10.2174/138527207781662519.

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36

Quine, J. R., M. T. Brenneman, and T. A. Cross. "Protein structural analysis from solid-state NMR-derived orientational constraints." Biophysical Journal 72, no. 5 (May 1997): 2342–48. http://dx.doi.org/10.1016/s0006-3495(97)78878-7.

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37

Gaudin, Etienne, Florent Boucher, Michel Evain, and Francis Taulelle. "NMR Selection of Space Groups in Structural Analysis of Ag7PSe6." Chemistry of Materials 12, no. 6 (June 2000): 1715–20. http://dx.doi.org/10.1021/cm001011u.

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38

Dommisse, Roger A., Lucia Van Hoof, and Arnold J. Vlietinck. "Structural analysis of phenolic glucosides from salicaceae by NMR spectroscopy." Phytochemistry 25, no. 5 (April 1986): 1201–4. http://dx.doi.org/10.1016/s0031-9422(00)81580-0.

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39

Kondrashova, Daria, and Rustem Valiullin. "Improving structural analysis of disordered mesoporous materials using NMR cryoporometry." Microporous and Mesoporous Materials 178 (September 2013): 15–19. http://dx.doi.org/10.1016/j.micromeso.2013.02.053.

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40

YEO, Joo-Hong, Makoto DEMURA, Takehito KONAKAZAWA, Tetsuo ASAKURA, Takuro ITOH, Teruaki FUJITO, and Tadashi IMANARI. "Structural Analysis of Polyamide Fibers by Solid State 15N NMR." KOBUNSHI RONBUNSHU 51, no. 1 (1994): 47–51. http://dx.doi.org/10.1295/koron.51.47.

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41

Pauli, Guido F., Shao-Nong Chen, David C. Lankin, Jonathan Bisson, Ryan J. Case, Lucas R. Chadwick, Tanja Gödecke, et al. "Essential Parameters for Structural Analysis and Dereplication by1H NMR Spectroscopy." Journal of Natural Products 77, no. 6 (June 4, 2014): 1473–87. http://dx.doi.org/10.1021/np5002384.

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42

Bechinger, Burkhard, Rudolf Kinder, Michael Helmle, Titus C. B. Vogt, Ulrike Harzer, and Susan Schinzel. "ChemInform Abstract: Peptide Structural Analysis by Solid-State NMR Spectroscopy." ChemInform 31, no. 9 (June 10, 2010): no. http://dx.doi.org/10.1002/chin.200009299.

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43

O'Connell, Mitchell R., Roland Gamsjaeger, and Joel P. Mackay. "The structural analysis of proteinâprotein interactions by NMR spectroscopy." PROTEOMICS 9, no. 23 (December 2009): 5224–32. http://dx.doi.org/10.1002/pmic.200900303.

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44

Geyer, A., G. Hummel, S. Reinhardt, and R. R. Schmidt. "ChemInform Abstract: NMR Analysis of a Rigid Carbohydrate Structural Motif." ChemInform 30, no. 16 (June 16, 2010): no. http://dx.doi.org/10.1002/chin.199916360.

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45

Carpentier, Claire E., Jeffrey M. Schreifels, Elena L. Aronovich, Daniel F. Carlson, Perry B. Hackett, and Irina V. Nesmelova. "NMR structural analysis of Sleeping Beauty transposase binding to DNA." Protein Science 23, no. 1 (November 18, 2013): 23–33. http://dx.doi.org/10.1002/pro.2386.

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46

TANAKA, T., and M. IKURA. "ChemInform Abstract: Structural Analysis of Proteins by Multi-Dimensional NMR." ChemInform 24, no. 46 (August 20, 2010): no. http://dx.doi.org/10.1002/chin.199346328.

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47

Tanaka, Y., T. Hori, M. Katahira, F. Nishikawa, T. Sakamoto, Y. Fukunaga, Y. Kurihara, S. Nishikawa, and S. Uesugi. "Design and NMR analysis of HDV ribozymes for structural investigation." Nucleic Acids Symposium Series 42, no. 1 (November 1, 1999): 221–22. http://dx.doi.org/10.1093/nass/42.1.221.

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48

Bailly, A., J. P. Amoureux, J. W. Wiench, and M. Pruski. "Structural Analysis of ZON-Type Aluminophosphates by Solid State NMR." Journal of Physical Chemistry B 105, no. 4 (February 2001): 773–76. http://dx.doi.org/10.1021/jp0027795.

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49

Espelie, Karl E., Frank A. Loewus, Ronald J. Pugmire, Warner R. Woolfenden, Bruce G. Baldi, and Peter H. Given. "Structural analysis of Lilium longiflorum sporopollenin by 13C NMR spectroscopy." Phytochemistry 28, no. 3 (January 1989): 751–53. http://dx.doi.org/10.1016/0031-9422(89)80108-6.

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50

Moore, G. R. "Carbon-13 NMR chemical shifts in structural and stereochemical analysis." Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 51, no. 13 (November 1995): 2428–29. http://dx.doi.org/10.1016/0584-8539(95)90091-8.

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