Article
Structure determination of uniformly (13)C, (15)N labeled protein using qualitative distance restraints from MAS solid-state (13)C-NMR observed paramagnetic relaxation enhancement.
Journal of biomolecular NMR - 1 Jan 2016
Tamaki Hajime, Egawa Ayako, Kido Kouki, Kameda Tomoshi, Kamiya Masakatsu, Kikukawa Takashi, Aizawa Tomoyasu, Fujiwara Toshimichi, Demura Makoto
Abstract excerpt
Magic angle spinning (MAS) solid-state nuclear magnetic resonance (NMR) is a powerful method for structure determination of insoluble biomolecules. However, structure determination by MAS solid-state NMR remains challenging because it is difficult to obtain a sufficient amount of distance restraints owing to spectral complexity. Collection of distance restraints from paramagnetic relaxation enhancement (PRE) is a...
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