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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
Autor:
Ann E. McDermott, Justin L. Lorieau
Publikováno v:
Journal of the American Chemical Society. 128:11505-11512
The majority of protein structures are determined in the crystalline state, yet few methods exist for the characterization of dynamics for crystalline biomolecules. Solid-state NMR can be used to probe detailed dynamic information in crystalline biom
Publikováno v:
Journal of the American Chemical Society. 129(10)
In this paper, we present a series of heteronuclear NMR experiments for the direct observation and characterization of lysine NH3 groups in proteins. In the context of the HoxD9 homeodomain bound specifically to DNA we were able to directly observe t
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.