通过固态核磁共振研究蛋白质动力学：fd噬菌体外壳蛋白的芳香环
Protein dynamics by solid-state NMR: aromatic rings of the coat protein in fd bacteriophage.
作者信息
Gall C M, Cross T A, DiVerdi J A, Opella S J
出版信息
Proc Natl Acad Sci U S A. 1982 Jan;79(1):101-5. doi: 10.1073/pnas.79.1.101.
Abstract
The motions of the aromatic amino acids of the fd bacteriophage coat protein are described by solid-state 2H, 13C, and 15N NMR. Tryptophan-26 is immobile on time scales as slow as 10(3) HZ. The phenylalanine and tyrosine rings undergo 180 degree flips about the C beta--C gamma bond axis more often than 10(6) HZ as well as small-amplitude rapid motions in other directions.
摘要
通过固态2H、13C和15N核磁共振描述了fd噬菌体外壳蛋白芳香族氨基酸的运动。色氨酸-26在低至10³赫兹的时间尺度上是不移动的。苯丙氨酸和酪氨酸环围绕Cβ-Cγ键轴进行180°翻转的频率高于10⁶赫兹，并且在其他方向上还有小幅度的快速运动。
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