Microsecond time scale mobility in a solid protein as studied by the 15N R(1rho) site-specific NMR relaxation rates.
Microsecond time scale mobility in a solid protein as studied by the 15N R(1rho) site-specific NMR relaxation rates.
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通过 15N R(1rho) 位点特异性 NMR 弛豫率研究固体蛋白质中微秒级的迁移率。
DOI：
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发表时间：
2010
影响因子：
15
通讯作者：
B. Reif
中科院分区：
文献类型：
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作者：
A. Krushelnitsky;T. Zinkevich;D. Reichert;Veniamin Chevelkov;B. Reif
这是第一次，我们已经证明了可靠的（即，（15）固体蛋白质的NR（1 ρ）弛豫速率，以提取微秒时间尺度上的动态信息。(15)N在鸡α-血影蛋白的（15）N，（2）H-富集（在不稳定位点具有10-20%的反向交换质子）微晶SH 3结构域中，测量作为残基数目的函数的R（1 rho）NMR弛豫速率。实验在不同的温度和不同的自旋锁频率下进行，这是通过共振和非共振自旋锁照射实现的。得到的结果表明，干扰自旋自旋贡献的R（1 ρ）率在全氘代蛋白质是可以忽略不计的，即使在低自旋锁领域，在正常质子化样品的情况下。通过相关图，R（1 rho）率与以前的数据进行了比较，相同的蛋白质表征不同种类的内部流动性。
For the first time, we have demonstrated the site-resolved measurement of reliable (i.e., free of interfering effects) (15)N R(1rho) relaxation rates from a solid protein to extract dynamic information on the microsecond time scale. (15)N R(1rho) NMR relaxation rates were measured as a function of the residue number in a (15)N,(2)H-enriched (with 10-20% back-exchanged protons at labile sites) microcrystalline SH3 domain of chicken alpha-spectrin. The experiments were performed at different temperatures and at different spin-lock frequencies, which were realized by on- and off-resonance spin-lock irradiation. The results obtained indicate that the interfering spin-spin contribution to the R(1rho) rate in a perdeuterated protein is negligible even at low spin-lock fields, in contrast to the case for normal protonated samples. Through correlation plots, the R(1rho) rates were compared with previous data for the same protein characterizing different kinds of internal mobility.
影响因子：
15
作者：
Gibson, JM;Popham, JM;Drobny, GP
通讯作者：
Drobny, GP