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Journal articles on the topic 'Function by NMR spectroscopy'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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1

Pfeffer, Philip E., Berta Bago, and Yair Shachar-Hill. "Exploring mycorrhizal function with NMR spectroscopy." New Phytologist 150, no. 3 (2001): 543–53. http://dx.doi.org/10.1046/j.1469-8137.2001.00139.x.

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2

Didenko, Tatiana, Afonso M. S. Duarte, G. Elif Karagöz, and Stefan G. D. Rüdiger. "Hsp90 structure and function studied by NMR spectroscopy." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1823, no. 3 (2012): 636–47. http://dx.doi.org/10.1016/j.bbamcr.2011.11.009.

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3

Goldberga, Ieva, Rui Li, and Melinda J. Duer. "Collagen Structure–Function Relationships from Solid-State NMR Spectroscopy." Accounts of Chemical Research 51, no. 7 (2018): 1621–29. http://dx.doi.org/10.1021/acs.accounts.8b00092.

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4

Bashta, Bogdana, Volodymyr Donchak, Marta Plonska-Brzezinskа, Olena Astakhova, and Michael Bratychak. "Investigation of Functional Carboxy-Containing Oligomers by IR and NMR Spectroscopy." Chemistry & Chemical Technology 10, no. 2 (2016): 125–34. http://dx.doi.org/10.23939/chcht10.02.125.

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New functional oligomers have been synthesized via intereaction of epoxy oligomers with carboxylic ones or with dibasic carboxy acids. In some cases synthesis was accompanied by ROP-polymerization of DGEBA, initiated by carboxylic oligomer. The structure of obtained products was investigated by IR, 1Н and 13C NMR spectroscopy.

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5

Gjuroski, Ilche, Julien Furrer, and Martina Vermathen. "Probing the Interactions of Porphyrins with Macromolecules Using NMR Spectroscopy Techniques." Molecules 26, no. 7 (2021): 1942. http://dx.doi.org/10.3390/molecules26071942.

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Porphyrinic compounds are widespread in nature and play key roles in biological processes such as oxygen transport in blood, enzymatic redox reactions or photosynthesis. In addition, both naturally derived as well as synthetic porphyrinic compounds are extensively explored for biomedical and technical applications such as photodynamic therapy (PDT) or photovoltaic systems, respectively. Their unique electronic structures and photophysical properties make this class of compounds so interesting for the multiple functions encountered. It is therefore not surprising that optical methods are typically the prevalent analytical tool applied in characterization and processes involving porphyrinic compounds. However, a wealth of complementary information can be obtained from NMR spectroscopic techniques. Based on the advantage of providing structural and dynamic information with atomic resolution simultaneously, NMR spectroscopy is a powerful method for studying molecular interactions between porphyrinic compounds and macromolecules. Such interactions are of special interest in medical applications of porphyrinic photosensitizers that are mostly combined with macromolecular carrier systems. The macromolecular surrounding typically stabilizes the encapsulated drug and may also modify its physical properties. Moreover, the interaction with macromolecular physiological components needs to be explored to understand and control mechanisms of action and therapeutic efficacy. This review focuses on such non-covalent interactions of porphyrinic drugs with synthetic polymers as well as with biomolecules such as phospholipids or proteins. A brief introduction into various NMR spectroscopic techniques is given including chemical shift perturbation methods, NOE enhancement spectroscopy, relaxation time measurements and diffusion-ordered spectroscopy. How these NMR tools are used to address porphyrin–macromolecule interactions with respect to their function in biomedical applications is the central point of the current review.

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6

Baker, Lindsay A., and Marc Baldus. "Characterization of membrane protein function by solid-state NMR spectroscopy." Current Opinion in Structural Biology 27 (August 2014): 48–55. http://dx.doi.org/10.1016/j.sbi.2014.03.009.

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7

Ruan, Ke-He. "High resolution nuclear magnetic resonance spectroscopy-guided mutagenesis for characterization of membrane-bound proteins: Experimental designs and applications." Spectroscopy 18, no. 1 (2004): 13–29. http://dx.doi.org/10.1155/2004/802728.

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High resolution Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for determining the solution structures of peptides and small proteins, and their ligand binding functions. Molecular biology mutagenesis is a widely used and powerful approach for identification of the protein functions. We have developed a strategy integrating NMR experiments with mutagenesis studies to advance and extend the approaches used for structure/function relationship studies of proteins, especially for membrane-bound proteins, which play important roles in physiopathological processes. The procedures include the design of the functional protein domain, identification of the solution structure and intermolecular contacts between the protein segment and its ligand. These determinations are resolved by high-resolution 2D NMR spectroscopy, and followed by site-directed mutagenesis of the residues suggested from the NMR experiment for the membrane-bound proteins. The residues important to the protein functions, identified by the mutagenesis, were further used to re-assign the NMR spectra and finalize the docking of the protein with its ligand. A structural model of the protein/ligand interaction can be constructed at an atomic level based on the NMR spectroscopy and mutagenesis results. As an application, the strategy has enhanced our knowledge in the understanding of the structure/function relationship for a membrane-bound G protein coupling receptor, the thromboxane A2receptor (TP receptor), interacting with its ligand, and a microsomal P450, prostacyclin synthase (PGIS), docking with its substrate in the endoplasmic reticulum (ER) membrane. In this review, we have summarized the principles and applications for this newly developed technique.

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8

Chance, B., and W. Bank. "Genetic disease of mitochondrial function evaluated by NMR and NIR spectroscopy of skeletal tissue." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1271, no. 1 (1995): 7–14. http://dx.doi.org/10.1016/0925-4439(95)00003-m.

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9

Lippens, Guy, Isabelle Landrieu, Caroline Smet, et al. "NMR Meets Tau: Insights into Its Function and Pathology." Biomolecules 6, no. 2 (2016): 28. http://dx.doi.org/10.3390/biom6020028.

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In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately linked to both aspects. NMR spectroscopy has depicted accurate phosphorylation patterns by different kinases, and its non-destructive character has allowed functional assays with the same samples. Finally, we will discuss other post-translational modifications of Tau and its interaction with other cellular factors in relationship to its (dys)function.

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10

Yonker, C. R., and S. L. Wallen. "High-Pressure On-Line Photolysis with NMR Detection." Applied Spectroscopy 50, no. 6 (1996): 781–84. http://dx.doi.org/10.1366/0003702963905664.

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The investigation of the photoreversible fulgide Aberchrome-540 as a function of pressure and temperature with the use of nuclear magnetic resonance (NMR) detection is described. This technique demonstrates the novel combination of high-pressure NMR and laser photolysis with the use of fiber optics for the conversion of the fulgide on-line in the instrument. Investigation of the photolysis of Aberchrome-540 to 2.0 kbar and 120 °C is reported. Extension of this technique should allow the investigation of photoinitiated reaction kinetics and equilibria as a function of pressure and temperature with simultaneous structure characterization by NMR.

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11

Varani, Gabriele, and Ignacio Tinoco. "RNA structure and NMR spectroscopy." Quarterly Reviews of Biophysics 24, no. 4 (1991): 479–532. http://dx.doi.org/10.1017/s0033583500003875.

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12

Goncalves, Joseph A., Shivani Ahuja, Sina Erfani, Markus Eilers, and Steven O. Smith. "Structure and function of G protein-coupled receptors using NMR spectroscopy." Progress in Nuclear Magnetic Resonance Spectroscopy 57, no. 2 (2010): 159–80. http://dx.doi.org/10.1016/j.pnmrs.2010.04.004.

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13

Quirion, G., C. Bourbonnais, E. Barthel, et al. "NMR spectroscopy in K3C60 as a function of temperature and pressure." Synthetic Metals 56, no. 2-3 (1993): 3154–59. http://dx.doi.org/10.1016/0379-6779(93)90095-e.

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14

Phang, P. T., D. L. Swinamer, R. Eccles, et al. "Muscle function testing and 31P-NMR spectroscopy in fasted healthy volunteers." Journal of Critical Care 2, no. 3 (1987): 156–61. http://dx.doi.org/10.1016/0883-9441(87)90002-5.

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15

Opella, S. J., A. Nevzorov, M. F. Mesleh, and F. M. Marassi. "Structure determination of membrane proteins by NMR spectroscopy." Biochemistry and Cell Biology 80, no. 5 (2002): 597–604. http://dx.doi.org/10.1139/o02-154.

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Current strategies for determining the structures of membrane proteins in lipid environments by NMR spectroscopy rely on the anisotropy of nuclear spin interactions, which are experimentally accessible through experiments performed on weakly and completely aligned samples. Importantly, the anisotropy of nuclear spin interactions results in a mapping of structure to the resonance frequencies and splittings observed in NMR spectra. Distinctive wheel-like patterns are observed in two-dimensional 1H15N heteronuclear dipolar/15N chemical shift PISEMA (polarization inversion spin-exchange at the magic angle) spectra of helical membrane proteins in highly aligned lipid bilayer samples. One-dimensional dipolar waves are an extension of two-dimensional PISA (polarity index slant angle) wheels that map protein structures in NMR spectra of both weakly and completely aligned samples. Dipolar waves describe the periodic wave-like variations of the magnitudes of the heteronuclear dipolar couplings as a function of residue number in the absence of chemical shift effects. Since weakly aligned samples of proteins display these same effects, primarily as residual dipolar couplings, in solution NMR spectra, this represents a convergence of solid-state and solution NMR approaches to structure determination.Key words: NMR spectroscopy, protein structure, dipolar couplings, membrane proteins, structure determination.

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16

Cooper, C. E., and J. S. Wyatt. "NMR spectroscopy and imaging of the neonatal brain." Biochemical Society Transactions 28, no. 2 (2000): 121–26. http://dx.doi.org/10.1042/bst0280121.

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Magnetic resonance spectroscopy and imaging provide unique information about the brain to the biochemist and the clinician. In particular, the ability to image metabolites other than water and to get detailed information about dynamic cellular processes (such as blood flow, blood oxygenation and cell swelling) is leading to many new insights into brain function and dysfunction. This review describes the use of old and new NMR techniques which demonstrate that mitochondrial dysfunction plays an important role in the cell death that occurs following an hypoxic-ischaemic insult to the neonatal brain.

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17

Liu, Juwhan, Antti O. K. Nieminen, and Jack L. Koenig. "Deconvolution of the Chemical Shift Effects in Proton Nuclear Magnetic Resonance Imaging." Applied Spectroscopy 43, no. 7 (1989): 1260–64. http://dx.doi.org/10.1366/0003702894203697.

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When the gradient strength is not strong enough to suppress the chemical shift effects, it is possible to apply a numerical deconvolution technique to remove the chemical shift artifacts. The Wiener filter and an apodization function are combined to produce an effective deconvolution method for the NMR images obtained by standard spin-echo NMR imaging technique. In the deconvolution process, an NMR spectrum is utilized which is taken at the same condition as the NMR image but with the phase encoding and the read gradients off.

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18

Landrieu, Isabelle, Arnaud Leroy, Caroline Smet-Nocca, et al. "NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease." Biochemical Society Transactions 38, no. 4 (2010): 1006–11. http://dx.doi.org/10.1042/bst0381006.

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NMR spectroscopy was used to explore the different aspects of the normal and pathological functions of tau, but proved challenging because the protein contains 441 amino acids and has poor signal dispersion. We have set out to dissect the phosphorylation patterns of tau in order to understand better its role in the aggregation process and microtubule-binding regulation. Our current knowledge on the functional consequences of specific phosphorylations is still limited, mainly because producing and assessing quantitatively phosphorylated tau samples is far from straightforward, even in vitro. We use NMR spectroscopy as a proteomics tool to characterize the phosphorylation patterns of tau, after in vitro phosphorylation by recombinant kinases. The phosphorylated tau can next be use for functional assays or interaction assays with phospho-dependent protein partners, such as the prolyl cis–trans isomerase Pin1.

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19

Miyatou, Tatsuya, Ryutaro Ohashi, Tomonori Ida, Shigeharu Kittaka, and Motohiro Mizuno. "An NMR study on the mechanisms of freezing and melting of water confined in spherically mesoporous silicas SBA-16." Physical Chemistry Chemical Physics 18, no. 27 (2016): 18555–62. http://dx.doi.org/10.1039/c6cp03111k.

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Thermodynamic and dynamic properties of water confined in mesoporous silica glass SBA-16 were investigated by DSC and <sup>1,2</sup>H NMR spectroscopy and <sup>2</sup>H NMR spin–lattice relaxation time as a function of pore size.

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20

Baker, Lindsay A., and Marc Baldus. "ChemInform Abstract: Characterization of Membrane Protein Function by Solid-state NMR Spectroscopy." ChemInform 46, no. 7 (2015): no. http://dx.doi.org/10.1002/chin.201507335.

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21

Traficante, Daniel D., and Gregory A. Nemeth. "A new and improved apodization function for resolution enhancement in NMR spectroscopy." Journal of Magnetic Resonance (1969) 71, no. 2 (1987): 237–45. http://dx.doi.org/10.1016/0022-2364(87)90053-9.

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22

Alderson, T. Reid, and Lewis E. Kay. "NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function." Cell 184, no. 3 (2021): 577–95. http://dx.doi.org/10.1016/j.cell.2020.12.034.

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23

Gupta, Rupal, Jenna Yehl, Mingyue Li, and Tatyana Polenova. "51V magic angle spinning NMR spectroscopy and quantum chemical calculations in vanadium bio-inorganic systems: current perspective." Canadian Journal of Chemistry 93, no. 9 (2015): 929–37. http://dx.doi.org/10.1139/cjc-2014-0557.

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In recent years, 51V magic angle spinning (MAS) NMR spectroscopy has been widely used to characterize vanadium centers in biology, biomimetic complexes, and inorganic compounds of medicinal and industrial relevance. It has been demonstrated that 51V NMR parameters are sensitive probes of the coordination geometry and chemical environment of the metal center, beyond the first coordination sphere. To establish the relationships between NMR parameters and structure of the vanadium centers, over the past decade a large series of coordination complexes have been analyzed by MAS NMR spectroscopy. It has been demonstrated that the interpretation of the NMR parameters requires the use of theoretical methods, such as density functional (DFT) theory, whereby the experimental NMR observables are linked to the electronic and structural properties of a molecule. DFT calculations have been successfully employed to not only predict NMR parameters but to also yield valuable information regarding the structure and function of various vanadium compounds. In this report, we review the current state of the field, and present a survey of bioinorganic vanadium complexes as well as vanadium-dependent haloperoxidases analyzed using 51V MAS NMR spectroscopy and DFT calculations, to illustrate the rich information content available from such a combined approach.

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24

Oh, Kwang-Im, Jinwoo Kim, Chin-Ju Park, and Joon-Hwa Lee. "Dynamics Studies of DNA with Non-canonical Structure Using NMR Spectroscopy." International Journal of Molecular Sciences 21, no. 8 (2020): 2673. http://dx.doi.org/10.3390/ijms21082673.

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The non-canonical structures of nucleic acids are essential for their diverse functions during various biological processes. These non-canonical structures can undergo conformational exchange among multiple structural states. Data on their dynamics can illustrate conformational transitions that play important roles in folding, stability, and biological function. Here, we discuss several examples of the non-canonical structures of DNA focusing on their dynamic characterization by NMR spectroscopy: (1) G-quadruplex structures and their complexes with target proteins; (2) i-motif structures and their complexes with proteins; (3) triplex structures; (4) left-handed Z-DNAs and their complexes with various Z-DNA binding proteins. This review provides insight into how the dynamic features of non-canonical DNA structures contribute to essential biological processes.

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25

Wacker, Anna, Julia E. Weigand, Sabine R. Akabayov, et al. "Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy." Nucleic Acids Research 48, no. 22 (2020): 12415–35. http://dx.doi.org/10.1093/nar/gkaa1013.

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Abstract The current pandemic situation caused by the Betacoronavirus SARS-CoV-2 (SCoV2) highlights the need for coordinated research to combat COVID-19. A particularly important aspect is the development of medication. In addition to viral proteins, structured RNA elements represent a potent alternative as drug targets. The search for drugs that target RNA requires their high-resolution structural characterization. Using nuclear magnetic resonance (NMR) spectroscopy, a worldwide consortium of NMR researchers aims to characterize potential RNA drug targets of SCoV2. Here, we report the characterization of 15 conserved RNA elements located at the 5′ end, the ribosomal frameshift segment and the 3′-untranslated region (3′-UTR) of the SCoV2 genome, their large-scale production and NMR-based secondary structure determination. The NMR data are corroborated with secondary structure probing by DMS footprinting experiments. The close agreement of NMR secondary structure determination of isolated RNA elements with DMS footprinting and NMR performed on larger RNA regions shows that the secondary structure elements fold independently. The NMR data reported here provide the basis for NMR investigations of RNA function, RNA interactions with viral and host proteins and screening campaigns to identify potential RNA binders for pharmaceutical intervention.

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26

Sikes, Patricia J., Piyu Zhao, David L. Maass, and Jureta W. Horton. "Time course of myocardial sodium accumulation after burn trauma: a 31P- and 23Na-NMR study." Journal of Applied Physiology 91, no. 6 (2001): 2695–702. http://dx.doi.org/10.1152/jappl.2001.91.6.2695.

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In this study,23Na- and 31P- nuclear magnetic resonance (NMR) spectra were examined in perfused rat hearts harvested 1, 2, 4, and 24 h after 40% total body surface area burn trauma and lactated Ringer resuscitation, 4 ml · kg−1 · %−1 burn.23Na-NMR spectroscopy monitored myocardial intracellular Na+ using the paramagnetic shift reagent thulium 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetra(methylenephosphonic acid). Left ventricular function, cardiac high-energy phosphates (ATP/PCr), and myocyte intracellular pH were studied by using31P NMR spectroscopy to examine the hypothesis that burn-mediated acidification of cardiomyocytes contributes to subsequent Na+ accumulation by this cell population. Intracellular Na+ accumulation was confirmed by sodium-binding benzofuran isophthalate loading and fluorescence spectroscopy in cardiomyocytes isolated 1, 2, 4, 8, 12, 18, and 24 h postburn. This myocyte Na+ accumulation as early as 2 h postburn occurred despite no changes in cardiac ATP/PCr and intracellular pH. Left ventricular function progressively decreased after burn trauma. Cardiomyocyte Na+ accumulation paralleled cardiac contractile dysfunction, suggesting that myocardial Na+overload contributes, in part, to the progressive postburn decrease in ventricular performance.

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27

Kim, Do-Hyoung, Jongchan Lee, K. Mok, Jung Lee, and Kyou-Hoon Han. "Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy." Biomolecules 10, no. 3 (2020): 428. http://dx.doi.org/10.3390/biom10030428.

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Elucidating the structural details of proteins is highly valuable and important for the proper understanding of protein function. In the case of intrinsically disordered proteins (IDPs), however, obtaining the structural details is quite challenging, as the traditional structural biology tools have only limited use. Nuclear magnetic resonance (NMR) is a unique experimental tool that provides ensemble conformations of IDPs at atomic resolution, and when studying IDPs, a slightly different experimental strategy needs to be employed than the one used for globular proteins. We address this point by reviewing many NMR investigations carried out on the α-synuclein protein, the aggregation of which is strongly correlated with Parkinson’s disease.

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28

Sinelnikova, Anna, and David van der Spoel. "NMR refinement and peptide folding using the GROMACS software." Journal of Biomolecular NMR 75, no. 4-5 (2021): 143–49. http://dx.doi.org/10.1007/s10858-021-00363-z.

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AbstractNuclear magnetic resonance spectroscopy is used routinely for studying the three-dimensional structures and dynamics of proteins and nucleic acids. Structure determination is usually done by adding restraints based upon NMR data to a classical energy function and performing restrained molecular simulations. Here we report on the implementation of a script to extract NMR restraints from a NMR-STAR file and export it to the GROMACS software. With this package it is possible to model distance restraints, dihedral restraints and orientation restraints. The output from the script is validated by performing simulations with and without restraints, including the ab initio refinement of one peptide.

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29

Djuandhi, Lisa, Neeraj Sharma, Bruce C. C. Cowie, Thanh V. Nguyen, and Aditya Rawal. "Elucidation of structures and lithium environments for an organo-sulfur cathode." Physical Chemistry Chemical Physics 21, no. 34 (2019): 18667–79. http://dx.doi.org/10.1039/c9cp03057c.

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30

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 challenging endeavor for most human GPCRs. We report a protocol for the production of the human histamine H1 receptor (H1R) in the methylotrophic yeast Pichia pastoris for NMR experiments. Systematic evaluation of multiple expression parameters resulted in a ten-fold increase in the yield of expressed H1R over initial efforts in defined media. The expressed receptor could be purified to homogeneity and was found to respond to the addition of known H1R ligands. Two-dimensional transverse relaxation-optimized spectroscopy (TROSY) NMR spectra of stable-isotope labeled H1R show well-dispersed and resolved signals consistent with a properly folded protein, and 19F-NMR data register a response of the protein to differences in efficacies of bound ligands.

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31

Bailey, R. E., R. A. Levine, J. Nandi, et al. "Effects of ethanol on gastric epithelial cell phospholipid dynamics and cellular function." American Journal of Physiology-Gastrointestinal and Liver Physiology 252, no. 2 (1987): G237—G243. http://dx.doi.org/10.1152/ajpgi.1987.252.2.g237.

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The lipid profile of isolated gastric superficial epithelial cells (SEC) was evaluated by proton nuclear magnetic resonance spectroscopy (1H-NMR). The most conspicuous resonance band in SEC spectra was due to the protons of +N(CH3)3 groups of phosphatidylcholine and, to a lesser degree, other phospholipid derivatives, on the basis of their chemical shift and addition of purified phospholipids. NMR of cell lysates and phospholipid extracts of SEC in deutero-chloroform provided further spectral resolution of these components. Phospholipase or ethanol treatments of SEC produced membrane disorganization reflected as increased peak intensity of the phospholipid signals. In addition, ethanol, in a dose-dependent manner, attenuated paranitrophenyl phosphatase activity, which correlated with inhibition of total and ouabain-sensitive 86Rubidium chloride uptake by SEC. This study suggests that NMR used in conjunction with other biochemical techniques can monitor SEC membrane structure-function relationships. NMR is a potentially powerful noninvasive probe to show changes in lipid membrane organization induced by low concentrations of ethanol (1%) and may indicate an early sign of "cytotoxicity" in intact SEC.

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32

Lisi, George P., and J. Patrick Loria. "Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function." Progress in Nuclear Magnetic Resonance Spectroscopy 92-93 (February 2016): 1–17. http://dx.doi.org/10.1016/j.pnmrs.2015.11.001.

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33

Tikhonova, Irina, and Stefano Costanzi. "Unraveling the Structure and Function of G Protein-Coupled Receptors Through NMR Spectroscopy." Current Pharmaceutical Design 15, no. 35 (2009): 4003–16. http://dx.doi.org/10.2174/138161209789824803.

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34

Foxall, Peta J. D., George J. Mellotte, Michael R. Bending, John C. Lindon, and Jeremy K. Nicholson. "NMR spectroscopy as a novel approach to the monitoring of renal transplant function." Kidney International 43, no. 1 (1993): 234–45. http://dx.doi.org/10.1038/ki.1993.37.

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35

Al-Hashimi, Hashim M. "Dynamics-Based Amplification of RNA Function and Its Characterization by Using NMR Spectroscopy." ChemBioChem 6, no. 9 (2005): 1506–19. http://dx.doi.org/10.1002/cbic.200500002.

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36

Korhonen, A., M. Ala-korpela, M. J. Liinamaa, J. Jokisaari, Y. A. Kesäniemi, and M. J. Savolainen. "Assessment of cholesteryl ester transfer protein function in lipoprotein mixtures by1H NMR spectroscopy." NMR in Biomedicine 10, no. 7 (1997): 303–8. http://dx.doi.org/10.1002/(sici)1099-1492(199710)10:7<303::aid-nbm482>3.0.co;2-o.

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37

Nunnally, Ray L., Evelyn E. Babcock, Sherye D. Horner, and Ronald M. Peshock. "Flourine-19 NMR spectroscopy and imaging investigations of myocardial perfusion and cardiac function." Magnetic Resonance Imaging 3, no. 4 (1985): 399–405. http://dx.doi.org/10.1016/0730-725x(85)90404-7.

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38

Tkadlecová, Marcela, Jaroslav Havlíček, and Vladimír Dohnal. "Association between halothane and oxygenated solvents by 1H NMR spectroscopy." Canadian Journal of Chemistry 73, no. 9 (1995): 1406–11. http://dx.doi.org/10.1139/v95-175.

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Using 1H NMR spectroscopy the complex-formation equilibria between halothane (2-bromo-2-chloro-1,1,1-trifluoroethane) and methyl tert-butyl ether or tetrahydrofuran in various inert solvents (hexane, heptane, decane, cyclohexane) were measured as a function of temperature. For two different association models (ideal solution and athermal solution), assuming only the formation of a 1:1 H-bonded complex, the equilibrium constants and the standard enthalpies of the complex-formation reaction were calculated. The ideal solution model provides values of the equilibrium constant that differ for different inert solvents. The athermal solution model makes this false solvent effect much smaller. For the low halothane concentration used, its dimerization was neglected. This assumption was verified experimentally. Keywords: 1H NMR, association, complex formation, halothane.

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39

Traficante, Daniel D., and Masoumeh Rajabzadeh. "Optimum window function for sensitivity enhancement of NMR signals." Concepts in Magnetic Resonance 12, no. 2 (2000): 83–101. http://dx.doi.org/10.1002/(sici)1099-0534(2000)12:2<83::aid-cmr3>3.0.co;2-h.

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40

Zia, Komal, Talal Siddiqui, Saqib Ali, Imran Farooq, Muhammad Sohail Zafar, and Zohaib Khurshid. "Nuclear Magnetic Resonance Spectroscopy for Medical and Dental Applications: A Comprehensive Review." European Journal of Dentistry 13, no. 01 (2019): 124–28. http://dx.doi.org/10.1055/s-0039-1688654.

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AbstractNuclear magnetic resonance (NMR) spectroscopy is one of the most significant analytical techniques that has been developed in the past few decades. A broad range of biological and nonbiological applications ranging from an individual cell to organs and tissues has been investigated through NMR. Various aspects of this technique are still under research, and many functions of the NMR are still pending a better understanding and acknowledgment. Therefore, this review is aimed at providing a general overview of the main principles, types of this technique, and the advantages and disadvantages of NMR spectroscopy. In addition, an insight into the current uses of NMR in the field of medicine and dentistry and ongoing developments of NMR spectroscopy for future applications has been discussed.

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41

Bartels, Christian, and Kurt W�thrich. "A spectral correlation function for efficient sequential NMR assignments of uniformly 15N-labeled proteins." Journal of Biomolecular NMR 4, no. 6 (1994): 775–85. http://dx.doi.org/10.1007/bf00398408.

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Smith, B. J., and V. A. Patrick. "Quantitative Determination of Sodium Dodecatungstosilicate Speciation by 183W Nuclear Magnetic Resonance Spectroscopy." Australian Journal of Chemistry 55, no. 4 (2002): 281. http://dx.doi.org/10.1071/ch01092.

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The speciation and equilibria of sodium dodecatungstosilicate has been determined using 183W nuclear magnetic resonance (NMR) spectroscopy over the pH range 3-13.5. The use of NMR allowed the direct observation of polytungstate anions in aqueous solution and at high concentration (0.5 mol L-1). Using this technique, the speciation of α-[SiW12O40]4-, α-[SiW11O39]8-, α-[NaSiW11O39]7-, α-[H2W12O40]6-, [H8W11O40]6-, [H7W11O40]7-, [W7O24]6-, [H2W12O42]10-, and WO42- was quantified as a function of pH. This work has allowed stability constants for α-[SiW12O40]4- (log K 46) and α-[SiW11O39]8- (log K 86) to be estimated.

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Hotchkiss, R. S., S. K. Song, C. S. Ling, J. J. Ackerman, and I. E. Karl. "Sepsis does not alter red blood cell glucose metabolism or Na+ concentration: a 2H-, 23Na-NMR study." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 258, no. 1 (1990): R21—R31. http://dx.doi.org/10.1152/ajpregu.1990.258.1.r21.

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The effects of sepsis on intracellular Na+ concentration ([Na+]i) and glucose metabolism were examined in rat red blood cells (RBCs) by using 23Na- and 2H-nuclear magnetic resonance (NMR) spectroscopy. Sepsis was induced in 15 halothane-anesthetized female Sprague-Dawley rats by using the cecal ligation and perforation technique; 14 control rats underwent cecal manipulation without ligation. The animals were fasted for 36 h, but allowed free access to water. At 36 h postsurgery, RBCs were examined by 23Na-NMR by using dysprosium tripolyphosphate as a chemical shift reagent. Human RBCs from 17 critically ill nonseptic patients and from 7 patients who were diagnosed as septic were also examined for [Na+]i. Five rat RBC specimens had [Na+]i determined by both 23Na-NMR and inductively coupled plasma-atomic emission spectroscopy (ICP-AES). For glucose metabolism studies, RBCs from septic and control rats were suspended in modified Krebs-Henseleit buffer containing [6,6-2H2]glucose and examined by 2H-NMR. No significant differences in [Na+]i or glucose utilization were found in RBCs from control or septic rats. There were no differences in [Na+]i in the two groups of patients. The [Na+]i determined by NMR spectroscopy agreed closely with measurements using ICP-AES and establish that 100% of the [Na+]i of the RBC is visible by NMR. Glucose measurements determined by 2H-NMR correlated closely (correlation coefficient = 0.93) with enzymatic analysis. These studies showed no evidence that sepsis disturbed RBC membrane function or metabolism.

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Harris, Kenneth D. M., Colan E. Hughes, P. Andrew Williams, and Gregory R. Edwards-Gau. "`NMR Crystallization': in-situ NMR techniques for time-resolved monitoring of crystallization processes." Acta Crystallographica Section C Structural Chemistry 73, no. 3 (2017): 137–48. http://dx.doi.org/10.1107/s2053229616019811.

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Solid-state NMR spectroscopy is a well-established and versatile technique for studying the structural and dynamic properties of solids, and there is considerable potential to exploit the power and versatility of solid-state NMR for in-situ studies of chemical processes. However, a number of technical challenges are associated with adapting this technique for in-situ studies, depending on the process of interest. Recently, an in-situ solid-state NMR strategy for monitoring the evolution of crystallization processes has been developed and has proven to be a promising approach for identifying the sequence of distinct solid forms present as a function of time during crystallization from solution, and for the discovery of new polymorphs. The latest development of this technique, called `CLASSIC' NMR, allows the simultaneous measurement of both liquid-state and solid-state NMR spectra as a function of time, thus yielding complementary information on the evolution of both the liquid phase and the solid phase during crystallization from solution. This article gives an overview of the range of NMR strategies that are currently available for in-situ studies of crystallization processes, with examples of applications that highlight the potential of these strategies to deepen our understanding of crystallization phenomena.

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Tokunaga, Yuji, Thibault Viennet, Haribabu Arthanari, and Koh Takeuchi. "Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR." International Journal of Molecular Sciences 21, no. 5 (2020): 1829. http://dx.doi.org/10.3390/ijms21051829.

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Solution NMR spectroscopy is a unique and powerful technique that has the ability to directly connect the structural dynamics of proteins in physiological conditions to their activity and function. Here, we summarize recent studies in which solution NMR contributed to the discovery of relationships between key dynamic properties of proteins and functional mechanisms in important biological systems. The capacity of NMR to quantify the dynamics of proteins over a range of time scales and to detect lowly populated protein conformations plays a critical role in its power to unveil functional protein dynamics. This analysis of dynamics is not only important for the understanding of biological function, but also in the design of specific ligands for pharmacologically important proteins. Thus, the dynamic view of structure provided by NMR is of importance in both basic and applied biology.

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Schöpel, Miriam, Veena Nambiar Potheraveedu, Thuraya Al-Harthy, Raid Abdel-Jalil, Rolf Heumann, and Raphael Stoll. "The small GTPases Ras and Rheb studied by multidimensional NMR spectroscopy: structure and function." Biological Chemistry 398, no. 5-6 (2017): 577–88. http://dx.doi.org/10.1515/hsz-2016-0276.

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Abstract Ras GTPases are key players in cellular signalling because they act as binary switches. These states manifest through toggling between an active (GTP-loaded) and an inactive (GDP-loaded) form. The hydrolysis and replenishing of GTP is controlled by two additional protein classes: GAP (GTPase-activating)- and GEF (Guanine nucleotide exchange factors)-proteins. The complex interplay of the proteins is known as the GTPase-cycle. Several point mutations of the Ras protein deregulate this cycle. Mutations in Ras are associated with up to one-third of human cancers. The three isoforms of Ras (H, N, K) exhibit high sequence similarity and mainly differ in a region called HVR (hypervariable region). The HVR governs the differential action and cellular distribution of the three isoforms. Rheb is a Ras-like GTPase that is conserved from yeast to mammals. Rheb is mainly involved in activation of cell growth through stimulation of mTORC1 activity. In this review, we summarise multidimensional NMR studies on Rheb and Ras carried out to characterise their structure-function relationship and explain how the activity of these small GTPases can be modulated by low molecular weight compounds. These might help to design GTPase-selective antagonists for treatment of cancer and brain disease.

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Hsu, Victor L., Xin Jia, and David R. Kearns. "Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor." Toxicology Letters 82-83 (December 1995): 577–89. http://dx.doi.org/10.1016/0378-4274(95)03585-0.

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Huang, Rui, Zev A. Ripstein, John L. Rubinstein, and Lewis E. Kay. "Cooperative subunit dynamics modulate p97 function." Proceedings of the National Academy of Sciences 116, no. 1 (2018): 158–67. http://dx.doi.org/10.1073/pnas.1815495116.

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p97 is an essential hexameric AAA+ ATPase involved in a wide range of cellular processes. Mutations in the enzyme are implicated in the etiology of an autosomal dominant neurological disease in which patients are heterozygous with respect to p97 alleles, containing one copy each of WT and disease-causing mutant genes, so that, in vivo, p97 molecules can be heterogeneous in subunit composition. Studies of p97 have, however, focused on homohexameric constructs, where protomers are either entirely WT or contain a disease-causing mutation, showing that for WT p97, the N-terminal domain (NTD) of each subunit can exist in either a down (ADP) or up (ATP) conformation. NMR studies establish that, in the ADP-bound state, the up/down NTD equilibrium shifts progressively toward the up conformation as a function of disease mutant severity. To understand NTD functional dynamics in biologically relevant p97 heterohexamers comprising both WT and disease-causing mutant subunits, we performed a methyl-transverse relaxation optimized spectroscopy (TROSY) NMR study on a series of constructs in which only one of the protomer types is NMR-labeled. Our results show positive cooperativity of NTD up/down equilibria between neighboring protomers, allowing us to define interprotomer pathways that mediate the allosteric communication between subunits. Notably, the perturbed up/down NTD equilibrium in mutant subunits is partially restored by neighboring WT protomers, as is the two-pronged binding of the UBXD1 adaptor that is affected in disease. This work highlights the plasticity of p97 and how subtle perturbations to its free-energy landscape lead to significant changes in NTD conformation and adaptor binding.

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Zhang, Zhenhong, Xiaohong Meng, Wei Cui, Syed S. Ahmad, Mohammad A. Kamal, and Jinguo Zhang. "NMR: From Molecular Mechanism to its Application in Medical Care." Medicinal Chemistry 16, no. 8 (2020): 1089–98. http://dx.doi.org/10.2174/1573406415666191111141630.

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Background: Nuclear Magnetic Resonance (NMR) spectroscopy is a systematic science strategy utilized in pharmaceutical research, development, quality control, and research to decide the content and purity of a sample as well as its sub-atomic structure. There are several parameters working for better execution of NMR which can include chemical shifts, spin multiplicity, pH dependence, heteronuclear and homonuclear covalent network, and the atomic overhauser impact. NMR imaging offers an extensive scope of potential outcomes for the portrayal of skeletal muscle structure, function and metabolism. 1H additionally has the most noteworthy NMR affectability of any nucleus. The principle of NMR depends on the spins of atomic nuclei. The magnetic estimations rely on an unpaired electron, while NMR estimates attractive impact brought about by the turn of protons and neutrons. The nucleons have intrinsic angular momenta or spins, which is considered as basic magnet. Conclusion: The presence of atomic attraction was uncovered in the hyperfine structure of spectral lines. If the nucleus magnetic moment is put in the magnetic field, the phenomenon of space quantization can be observed and each allowed direction will have a marginally unique energy level. Invitro, high-resolution NMR spectroscopy helps to assess tumor metabolism by the investigation of body liquids like urine, blood and removed tissue specimens. In-cell NMR is a powerful technique to assess strong compounds in medication improvement to spare exploratory expenses.

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Rittner, F., A. Seidel, T. Sprang, and B. Boddenberg. "129Xe NMR Linewidths as Indicators of Spatial Inhomogeneities in Zeolites." Applied Spectroscopy 50, no. 11 (1996): 1389–94. http://dx.doi.org/10.1366/0003702963904818.

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The widths of the 129Xe nuclear magnetic resonance (NMR) lines of xenon in zinc- and cadmium-exchanged zeolites NaY and HY were measured at ambient temperature as a function of the xenon gas equilibrium pressure. It is demonstrated that the observed values of the linewidths as well as their quite different dependence on pressure can be explained on the basis of a theoretical approach which traces back the origin of line broadening to inhomogeneous spatial distributions of transition metal cation sites interacting strongly with the encaged xenon atoms.

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