Добірка наукової літератури з теми "SsNMR spectroscopy"
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Статті в журналах з теми "SsNMR spectroscopy"
He, Lichun, Benjamin Bardiaux, Mumdooh Ahmed, Johannes Spehr, Renate König, Heinrich Lünsdorf, Ulfert Rand, Thorsten Lührs, and Christiane Ritter. "Structure determination of helical filaments by solid-state NMR spectroscopy." Proceedings of the National Academy of Sciences 113, no. 3 (January 5, 2016): E272—E281. http://dx.doi.org/10.1073/pnas.1513119113.
Повний текст джерелаvan der Wel, Patrick C. A. "New applications of solid-state NMR in structural biology." Emerging Topics in Life Sciences 2, no. 1 (February 23, 2018): 57–67. http://dx.doi.org/10.1042/etls20170088.
Повний текст джерелаRobin, Marc, Stanislas Von Euw, Guillaume Renaudin, Sandrine Gomes, Jean-Marc Krafft, Nadine Nassif, Thierry Azaïs, and Guylène Costentin. "Insights into OCP identification and quantification in the context of apatite biomineralization." CrystEngComm 22, no. 16 (2020): 2728–42. http://dx.doi.org/10.1039/c9ce01972c.
Повний текст джерелаMiddleton, D. A. "Solid-state NMR spectroscopy as a tool for drug design: from membrane-embedded targets to amyloid fibrils." Biochemical Society Transactions 35, no. 5 (October 25, 2007): 985–90. http://dx.doi.org/10.1042/bst0350985.
Повний текст джерелаSreemantula, Arun Kumar, and Alexander Marchanka. "Solid-state NMR spectroscopy for characterization of RNA and RNP complexes." Biochemical Society Transactions 48, no. 3 (June 23, 2020): 1077–87. http://dx.doi.org/10.1042/bst20191080.
Повний текст джерелаAder, C., R. Schneider, K. Seidel, M. Etzkorn, and M. Baldus. "Magic-angle-spinning NMR spectroscopy applied to small molecules and peptides in lipid bilayers." Biochemical Society Transactions 35, no. 5 (October 25, 2007): 991–95. http://dx.doi.org/10.1042/bst0350991.
Повний текст джерелаZhao, Li, Wei Li, Andreas Plog, Yeping Xu, Gerd Buntkowsky, Torsten Gutmann, and Kai Zhang. "Multi-responsive cellulose nanocrystal–rhodamine conjugates: an advanced structure study by solid-state dynamic nuclear polarization (DNP) NMR." Phys. Chem. Chem. Phys. 16, no. 47 (2014): 26322–29. http://dx.doi.org/10.1039/c4cp04096a.
Повний текст джерелаSiudem, Paweł, Jarosław Bukowicki, Iwona Wawer, and Katarzyna Paradowska. "Structural studies of two capsaicinoids: dihydrocapsaicin and nonivamide. 13C and 15N MAS NMR supported by genetic algorithm and GIAO DFT calculations." RSC Advances 10, no. 31 (2020): 18082–92. http://dx.doi.org/10.1039/d0ra01320j.
Повний текст джерелаZhao, Sha, Yufei Yang, Yujie Zhao, Xinming Li, Yi Xue, and Shenlin Wang. "High-resolution solid-state NMR spectroscopy of hydrated non-crystallized RNA." Chemical Communications 55, no. 93 (2019): 13991–94. http://dx.doi.org/10.1039/c9cc06552k.
Повний текст джерелаMandala, Venkata S., Jonathan K. Williams, and Mei Hong. "Structure and Dynamics of Membrane Proteins from Solid-State NMR." Annual Review of Biophysics 47, no. 1 (May 20, 2018): 201–22. http://dx.doi.org/10.1146/annurev-biophys-070816-033712.
Повний текст джерелаДисертації з теми "SsNMR spectroscopy"
Shannon, Matthew D. "High Resolution Structural and Dynamic Studies of Biomacromolecular Assemblies using Solid-State NMR Spectroscopy." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu1534321838601796.
Повний текст джерелаItkin, Anna. "Multidisniplinary study of Alzheimer's disease-related peptides : from amyloid precursor protein (APP) to amyloid β-oligomers and γ-secretase modulators". Thesis, Strasbourg, 2012. http://www.theses.fr/2012STRAF051/document.
Повний текст джерелаA histopathological characteristic of Alzheimer’s disease (AD) is the presence of amyloid plaques formed by amyloid β(A) peptides of 40 and 42 residues-long, which are the cleavage products of APP by proteases. To understand the role of structural changes in the TM domain of APP, APP_TM4K peptides were studied in the lipid bilayer using ATR-FTIR and ssNMR. While the overall secondary structure of the APP_TM4K peptide is helical, conformational and orientational heterogeneity was observed for the y- and for the -cleavage sites, which may have implications for the cleavage mechanism and therefore the production of Aβ. Starting from its monomeric form, Aβ peptides aggregate into fibrils and / or oligomers, the latter being the most neurotoxic. We found that in the presence of Ca2 +, Aβ (1-40) preferably forms oligomers, whereas in the absence of a2 + Aβ (1-40) aggregates into fibrils. In samples without Ca2 +, ATR-FTIR shows conversion from antiparallel β sheet conformation of oligomers into parallel β sheets, characteristic of fibrils. These results led us to conclude that Ca2 +stimulates the formation of oligomers of Aβ (1-40), that have been implicated in the pathogenesis of AD. Position and precise orientation of two new drugs powerful modulators of γ-secretase benzyl-carprofen and carprofen sulfonyl in the lipid bilayer were obtained from neutron scattering and ssNMR experiments. These results indicate that carprofen-derivatives can directly interact with APP. Such interaction would interfere with proper APP-dimer formation, which is necessary for the sequential cleavage by β -secretase, diminishing or greatly reducing Aβ42 production
Stevens, J. S., S. J. Byard, Colin C. Seaton, G. Sadiq, R. J. Davey, and S. L. M. Schroeder. "Proton transfer and hydrogen bonding in the organic solid state: a combined XRD/XPS/ssNMR study of 17 organic acid–base complexes." 2013. http://hdl.handle.net/10454/10190.
Повний текст джерелаThe properties of nitrogen centres acting either as hydrogen-bond or Brønsted acceptors in solid molecular acid–base complexes have been probed by N 1s X-ray photoelectron spectroscopy (XPS) as well as 15N solid-state nuclear magnetic resonance (ssNMR) spectroscopy and are interpreted with reference to local crystallographic structure information provided by X-ray diffraction (XRD). We have previously shown that the strong chemical shift of the N 1s binding energy associated with the protonation of nitrogen centres unequivocally distinguishes protonated (salt) from hydrogen-bonded (co-crystal) nitrogen species. This result is further supported by significant ssNMR shifts to low frequency, which occur with proton transfer from the acid to the base component. Generally, only minor chemical shifts occur upon co-crystal formation, unless a strong hydrogen bond is formed. CASTEP density functional theory (DFT) calculations of 15N ssNMR isotropic chemical shifts correlate well with the experimental data, confirming that computational predictions of H-bond strengths and associated ssNMR chemical shifts allow the identification of salt and co-crystal structures (NMR crystallography). The excellent agreement between the conclusions drawn by XPS and the combined CASTEP/ssNMR investigations opens up a reliable avenue for local structure characterization in molecular systems even in the absence of crystal structure information, for example for non-crystalline or amorphous matter. The range of 17 different systems investigated in this study demonstrates the generic nature of this approach, which will be applicable to many other molecular materials in organic, physical, and materials chemistry.
EPSRC, Sanofi-Aventis
Частини книг з теми "SsNMR spectroscopy"
Paul, Subhradip, Hiroki Takahashi, Sabine Hediger, and Gaël De Paëpe. "Third Spin-Assisted Recoupling in SSNMR." In Annual Reports on NMR Spectroscopy, 93–142. Elsevier, 2015. http://dx.doi.org/10.1016/bs.arnmr.2014.12.003.
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