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Публикации

1. Izmailov, S. A., Rabdano, S. O., Hasanbasri, Z., Podkorytov, I. S., Saxena, S. & Skrynnikov, N. R.:
Structural and dynamic origins of ESR lineshapes in spin-labeled GB1 domain: the insights from spin dynamics simulations based on long MD trajectories. Sci Rep 10, 957 (2020).		 DOI
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2. Titov, A. A., Filippov, O. A., Smol’yakov, A. F., Godovikov, I. A., Shakirova, J. R., Tunik, S. P., Podkorytov, I. S. & Shubina, E. S.:
Luminescent Complexes of the Trinuclear Silver(I) and Copper(I) Pyrazolates Supported with Bis(diphenylphosphino)methane. Inorg. Chem. 58, 8645–8656 (2019).		 DOI
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3. Podkorytov, I. S., Cherkasova, T. G., Kayfadzhyan, E. A. & Varshavsky, Yu. S.:
Multiplet-Matched Filtering of 103Rh Signal Using Information Contained in 31P Spectrum of AA′XX′ 31P–103Rh Spin System. Appl Magn Reson 50, 563–568 (2019).		 DOI
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4. Kharkov, B., Duan, X., Tovar, E. S., Canary, J. W. & Jerschow, A.:
Singlet excitation in the intermediate magnetic equivalence regime and field-dependent study of singlet–triplet leakage. Physical Chemistry Chemical Physics 21, 2595–2600 (2019).		 DOI
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5. Varshavsky, Yu. S., Cherkasova, T. G., Galding, M. R., Korlyukov, A. A., Podkorytov, I. S., Gindin, V. A., Smirnov, S. N., Mazur, A. S. & Rubaylo, A. I.:
13C NMR spectrum of crystalline [Rh(Acac) (CO)2]: A contribution to the discussion on [Rh(Acac) (CO)2] molecular structure in the solid state. Journal of Organometallic Chemistry 874, 70–73 (2018).		 DOI
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6. Kharkov, B., Strouk, L., Skinner, T. E. & Jerschow, A.:
Optimal control RF pulses for excitation and suppression of NMR signals in a conductive medium. The Journal of Chemical Physics 149, 034201 (2018).		 DOI
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7. Kaempf, K., Izmailov, S. A., Rabdano, S. O., Groves, A. T., Podkorytov, I. S. & Skrynnikov, N. R.:
What Drives N-15 Spin Relaxation in Disordered Proteins? Combined NMR/MD Study of the H4 Histone Tail. Biophysical Journal 115, 2348–2367 (2018).		 DOI
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8. Jackalin, L., Kharkov, B. B., Komolkin, A. V. & Dvinskikh, S. V.:
Experimental strategies for 13 C– 15 N dipolar NMR spectroscopy in liquid crystals at the natural isotopic abundance. Physical Chemistry Chemical Physics 20, 22187–22196 (2018).		 DOI
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9. Dai, J., Kharkov, B. & Dvinskikh, S.:
Molecular and Segmental Orientational Order in a Smectic Mesophase of a Thermotropic Ionic Liquid Crystal. Crystals 9, 18 (2018).		 DOI
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10. Rogacheva, O. N., Izmailov, S. A., Slipchenko, L. V. & Skrynnikov, N. R.:
Non-native disulfide bridges in protein-peptide complex and in protein homodimers trigger unfolding and aggregation. The FEBS Journal 284 (Suppl. 1), 311 (2017).		 DOI
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11. Rogacheva, O. N., Izmailov, S. A., Slipchenko, L. V. & Skrynnikov, N. R.:
A new structural arrangement in proteins involving lysine NH3 + group and carbonyl. Scientific Reports 7, 16402 (2017).		 DOI
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12. Rabdano, S., Podkorytov, I., Luzik, D. & Skrynnikov, N.:
Characterizing the size of protein aggregate particles using a combination of NMR diffusion measurements and dynamic light scattering: case study of RRM2 domain from protein TDP-43. The FEBS Journal 284 (Suppl. 1), 212 (2017).		 DOI
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13. Rabdano, S. O., Izmailov, S. A., Luzik, D. A., Groves, A., Podkorytov, I. S. & Skrynnikov, N. R.:
Onset of disorder and protein aggregation due to oxidation-induced intermolecular disulfide bonds: case study of RRM2 domain from TDP-43. Scientific Reports 7, 11161 (2017).		 DOI
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14. Podkorytov, I. S., Belousov, M., Bondarev, S., Kaempf, K., Zhouravleva, G., Dvinskikh, S. V. & Skrynnikov, N. R.:
Detection of flexible portion of protein chain in Sup35NM amyloid fibrils by means of diffusion-filtered NMR experiment. The FEBS Journal 284 (Suppl. 1), 215 (2017).		 DOI
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15. Luzik, D. A., Rabdano, S. O. & Skrynnikov, N. R.:
Non-native disulfide bridges in protein-peptide complex and in protein homodimers trigger unfolding and aggregation. The FEBS Journal 284 (Suppl. 1), 212 (2017).		 DOI
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16. Kurauskas, V., Izmailov, S. A., Rogacheva, O. N., Hessel, A., Ayala, I., Woodhouse, J., Shilova, A., Xue, Y., Yuwen, T., Coquelle, N., Colletier, J.-P., Skrynnikov, N. R. & Schanda, P.:
Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Nature Communications 8, (2017).		 DOI
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17. Tyuryaeva, I. I., Lyublinskaya, O. G., Podkorytov, I. S. & Skrynnikov, N. R.:
Origin of anti-tumor activity of the cysteine-containing GO peptides and further optimization of their cytotoxic properties. Scientific Reports 7, 40217 (2017).		 DOI
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18. Solomatina, A. I., Chelushkin, P. S., Krupenya, D. V., Podkorytov, I. S., Artamonova, T. O., Sizov, V. V., Melnikov, A. S., Gurzhiy, V. V., Koshel, E. I., Shcheslavskiy, V. I., Tunik, S. P.:
Coordination to Imidazole Ring Switches on Phosphorescence of Platinum Cyclometalated Complexes:
The Route to Selective Labeling of Peptides and Proteins via Histidine Residues. Bioconjugate Chem. (2016).		 DOI
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19. Rogacheva, O. N., Izmailov, S. A., Kurauskas, V., Shilova, A., Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., Hessel, A., Woodhouse, J., Mikhailovskii, O., Willbold, D., Colletier, J., Skrynnikov, N. R., Schanda, P.:
Dynamics in Protein Crystals: Insights from MD Simulations Complement New Solid-State NMR and X-Ray Data. FEBS Journal 283, 237 (2016).		 DOI
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20. Yuwen, T., Xue, Y., Skrynnikov, N. R.:
Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets: 2. The Model of Encounter Complex Involving the Double Mutant of the c-Crk N-SH3 Domain and Peptide Sos. Biochemistry 55 (12), 1784–1800 (2016).		 DOI
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21. Rabdano, S. O., Podkorytov, I. S., Izmailov, S. A., Pivovarova, Y. V., Yakimov, A. P., Yuwen, T., Groves, A., Skrynnikov, N. R.:
Loss of Protein Stability due to Formation of Intermolecular Disulfide Bonds under the Effect of Oxidative Stress: Case Study of the RRM2 Domain from Neuropathological Protein TDP-43. Biophysical Journal 110 (3), 210a (2016).		 DOI
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22. Izmailov, S. A., Podkorytov, I. S., Skrynnikov, N. R.:
MD Modeling of Oxidative Folding in Peptides and Proteins. Biophysical Journal 110 (3), 644a–645a (2016).		 DOI
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23. Ledovskaya, M. S., Molchanov, A. P., Kostikov, R. R., Panikorovsky, T. L., Gurzhiy, V. V., Ryazantsev, M. N., Boitsov, V. M., Stepakov, A. V.:
Anthracene-Fused isoxazolopyrrolo[2,1-A]isoquinolines via an Endocyclic N-Acyliminium Ion Cyclization: A Joint Experimental and Theoretical Study. Tetrahedron 72 (32), 4827–4834 (2016).		 DOI
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24. Struts, A. V., Barmasov, A. V., Brown, M. F.:
Spectral Methods for Study of the G-Protein-Coupled Receptor Rhodopsin. II. Magnetic Resonance Methods. Opt. Spectrosc. 120 (2), 286–293 (2016).		 DOI
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25. Xu, X., Struts, A. V., Kumar Giri, A., Molugu, T. R., Guruge, C., Faylough, S., Nascimento, C. L., Nesnas, N., Hruby, V. J., Brown, M. F.:
Dynamics of Methyl Groups in Membrane Proteins Studied by Deterium Solid State NMR Relaxation. Biophysical Journal 110 (3), 73a (2016).		 DOI
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26. Struts, A. V., Xu, X., Molugu, T. R., Pitman, M. C., Faylough, S., Guruge, C., Nascimento, C., Nesnas, N., Brown, M. F.:
Retinal Chromophore Structure in Meta-II Rhodopsin Revealed by Solid-State 2H NMR and Molecular Modeling. Biophysical Journal 110 (3), 229a–230a (2016).		 DOI
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27. Perera, S. M. D. C., Shrestha, U., Bhowmik, D., Chawla, U., Struts, A. V., Chu, X., Brown, M. F.:
Neutron Scattering Reveals Protein Fluctuations in GPCR Activation. Biophysical Journal 110 (3), 228a–229a (2016).		 DOI
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28. Chawla, U., Perera, S. M. D. C., Struts, A. V., Pitman, M. C., Brown, M. F.:
Hydration Mediated G-Protein-Coupled Receptor Activation. Biophysical Journal 110 (3), 83a (2016).		 DOI
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29. Smekalova, T. N., Yatsishina, E. B., Garipov, A. S., Pasumanskii, A. E., Ketsko, R. S., Chudin, A. V.:
Natural Science Methods in Field Archaeology, with the Case Study of Crimea. Crystallogr. Rep. 61 (4), 533–542 (2016).		 DOI
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30. Shmyreva, A. A., Safdari, M., Furó, I., Dvinskikh, S. V.:
NMR Longitudinal Relaxation Enhancement in Metal Halides by Heteronuclear Polarization Exchange during Magic-Angle Spinning. The Journal of Chemical Physics 144 (22), 224201 (2016).		 DOI
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31. Kharkov, B. B., Chizhik, V. I., Dvinskikh, S. V.:
Broadband Cross-Polarization-Based Heteronuclear Dipolar Recoupling for Structural and Dynamic NMR Studies of Rigid and Soft Solids. The Journal of Chemical Physics 144 (3), 34201 (2016).		 DOI
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32. Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., Mikhailovskii, O., Willbold, D., Colletier, J.-P., Skrynnikov, N. R., Schanda, P.:
Observing the Overall Rocking Motion of a Protein in a Crystal. Nature Communications 6, 8361 (2015).		 DOI
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33. Abrahamsson, C., Nordstierna, L., Nordin, M., Dvinskikh, S. V. & Nydén, M.:
Magnetic orientation of nontronite clay in aqueous dispersions and its effect on water diffusion. Journal of Colloid and Interface Science 437, 205–210 (2015).		 DOI
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34. Gerts, E. D., Komolkin, A. V., Burmistrov, V. A., Alexandriysky, V. V. & Dvinskikh, S. V.:
Comparative study of local structure of two cyanobiphenyl liquid crystals by molecular dynamics method. The Journal of Chemical Physics 141, 074503 (2014).		 DOI
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35. Kharkov, B. B., Corkery, R. W. & Dvinskikh, S. V.:
Phase Transitions and Chain Dynamics of Surfactants Intercalated into the Galleries of Naturally Occurring Clay Mineral Magadiite. Langmuir 30, 7859–7866 (2014).		 DOI
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36. Xue, Y. & Skrynnikov, N. R.:
Ensemble MD simulations restrained via crystallographic data: Accurate structure leads to accurate dynamics: Ensemble MD Simulations. Protein Science 23, 488–507 (2014).		 DOI
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37. Yuwen, T. & Skrynnikov, N. R.:
CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions. Journal of Biomolecular NMR 58, 175–192 (2014).		 DOI
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38. Xu, X., Struts, A. V. & Brown, M. F.:
Generalized Model-Free Analysis of Nuclear Spin Relaxation Experiments. eMagRes, 2014, Vol 3: 275–286.		 DOI
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39. Brown, M. F. & Struts, A. V.:
Retinal in Rhodopsin Activation Viewed by Solid-State 2H NMR Spectroscopy. In New Developments in NMR, F. Separovic, and A. Naito, eds. (Cambridge: Royal Society of Chemistry), 320–352 (2014).		 DOI
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40. Kharkov, B. B., Chizhik, V. I. & Dvinskikh, S. V.:
Probing Molecular Mobility in Nanostructured Composites by Heteronuclear Dipolar NMR Spectroscopy. The Journal of Physical Chemistry C 118, 28308–28313 (2014).		 DOI
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41. Xue, Y., Yuwen, T., Zhu, F. & Skrynnikov, N. R.:
Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets. 1. NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the Peptide Sos. Biochemistry 53, 6473–6495 (2014).		 DOIPDF