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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. 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.