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Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies

✍ Scribed by M.F. Mesleh; K.G. Valentine; S.J. Opella; J.M. Louis; A.M. Gronenborn


Book ID
110413032
Publisher
Springer Netherlands
Year
2003
Tongue
English
Weight
135 KB
Volume
25
Category
Article
ISSN
0925-2738

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## Abstract The high resolution offered by magic‐angle spinning (MAS), when compared to the static condition in solid‐state NMR of powders, has been used to full advantage in a ^14^N MAS NMR study of some ammonium salts: CH~3~NH~3~Cl, (NH~4~)~2~(COO)~2~Β·H~2~O, (CH~3~)~3~(C~6~H~5~CH~2~)NCl, (CH~3~)~