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Direct Experimental Evidence of Surface-induced Protein Unfolding at the Single-molecule Level

Published online by Cambridge University Press:  30 July 2020

Evgeny Dubrovin ,
Nikolay Barinov ,
Tilman Schäffer  and
Dmitry Klinov
Evgeny Dubrovin
Affiliation:
FRCC of Physical-Chemical Medicine of FMBA; Lomonosov Moscow State University; NUST MISIS, Moscow, Moskva, Russia
Nikolay Barinov
Affiliation:
FRCC of Physical-Chemical Medicine of FMBA; Lomonosov Moscow State University; NUST MISIS, Moscow, Moskva, Russia
Tilman Schäffer
Affiliation:
University of Tübingen, Tübingen, Baden-Wurttemberg, Germany
Dmitry Klinov
Affiliation:
FRCC of Physical-Chemical Medicine of FMBA; Lomonosov Moscow State University; NUST MISIS, Moscow, Moskva, Russia

Abstract

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Type
3D Structures: From Macromolecular Assemblies to Whole Cells (3DEM FIG)
Information
Microscopy and Microanalysis , Volume 26 , Supplement S2 , August 2020 , pp. 312 - 313
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Copyright
Copyright © Microscopy Society of America 2020

References

Matouschek, A., Current Opinion in Structural Biology, 2003, 13, 98–109.10.1016/S0959-440X(03)00010-1CrossRefGoogle Scholar
Gehde, N., Hinrichs, C., Montilla, I., Charpian, S., Lingelbach, K. and Przyborski, J. M., Molecular Microbiology, 2009, 71, 613–628.10.1111/j.1365-2958.2008.06552.xCrossRefGoogle Scholar
Marx, G., Mou, X., Hotovely-Salomon, A., Levdansky, L., Gaberman, E., Belenky, D. and Gorodetsky, R., J. Biomed. Mater. Res., 2008, 84B, 49–57.10.1002/jbm.b.30842CrossRefGoogle Scholar
Sivaraman, B. and Latour, R. A., Biomaterials, 2010, 31, 832–839.10.1016/j.biomaterials.2009.10.008CrossRefGoogle Scholar
Chodankar, S., Aswal, V. K., Kohlbrecher, J., Vavrin, R. and Wagh, A. G., Phys. Rev. E, 2008, 77, 031901.10.1103/PhysRevE.77.031901CrossRefGoogle Scholar
Coglitore, D., J.-M. Janot and S. Balme, Advances in Colloid and Interface Science, 2019, 270, 278–292.10.1016/j.cis.2019.07.004CrossRefGoogle Scholar
Horbett, T. A., Journal of Biomedical Materials Research Part A, 2018, 106, 2777–2788.10.1002/jbm.a.36460CrossRefGoogle Scholar
Ferrari, A. C., et al. , Nanoscale, 2015, 7, 4598–4810.10.1039/C4NR01600ACrossRefGoogle Scholar
The work was partially supported by the Russian Science Foundation [17-75-30064] (investigation of fibrinogen unfolding) and by the Ministry of Education and Science of the Russian Federation in the framework of increase Competitiveness Program of NUST „MISIS”, implemented by a governmental decree dated 16th of March 2013, No 211 (analysis of RNAP unfolding).Google Scholar