Zobrazeno 1 - 4
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pro vyhledávání: '"35"'
Autor:
Aneel K. Aggarwal, Nicolas Bolik-Coulon, Fabien Ferrage, Ludovic Carlier, Philippe Pelupessy, Guillaume Bouvignies, Cyril Charlier, Sandrine Sagan, Rodrigue Marquant, Mikhail Kozlov, Astrid Walrant, Pablo De Ioannes, Patricia Cortes
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
Journal of the American Chemical Society, American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
Journal of the American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
Journal of the American Chemical Society, American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
International audience; Many intrinsically disordered proteins (IDPs) and protein regions (IDRs) engage in transient, yet specific, interactions with a variety of protein partners. Often, if not always, interactions with a protein partner lead to par
Publikováno v:
Journal of the American Chemical Society. 124:6449-6460
In the previous paper in this issue we have demonstrated that it is possible to measure the five different relaxation rates of a deuteron in (13)CH(2)D methyl groups of (13)C-labeled, fractionally deuterated proteins. The extensive set of data acquir
Autor:
Fiala, R., Spackova, N., Foldynová-Trantírková, S., Sponer, J., Sklenár, V., Trantirek, L., Cellular Protein Chemistry, Sub Cellular Protein Chemistry
Publikováno v:
Journal of the American Chemical Society, 133(35), 13790. American Chemical Society
In this work, a novel NMR method for the identification of preferential coordination sites between physiologically relevant counterions and nucleic acid bases is demonstrated. In this approach, the NMR cross-correlated relaxation rates between the ar
Publikováno v:
Journal of the American Chemical Society. 125(47)
Conformational changes occurring on the microsecond-millisecond time scale in basic pancreatic trypsin inhibitor (BPTI) are investigated using nuclear magnetic resonance spectroscopy. The rczz CPMG experiment (Wang, C.; Grey, M. J.; Palmer, A. G. J.