Deuterated peptides and proteins: structure and dynamics studies by MAS solid-state NMR.
作者： Bernd Reif
DOI: 10.1007/978-1-61779-480-3_16
关键词:
摘要: Perdeuteration and back substitution of exchangeable protons in microcrystalline proteins, combination with recrystallization from D(2)O-containing buffers, significantly reduce (1)H, (1)H dipolar interactions. This way, amide proton line widths on the order 20 Hz are obtained. Aliphatic accessible either via specifically protonated precursors or by using low amounts H(2)O bacterial growth medium. The labeling scheme enables characterization structure dynamics solid-state without truncation artifacts.
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