Effect of deuteration on some structural parameters of methyl groups in proteins as evaluated by residual dipolar couplings
Effect of deuteration on some structural parameters of methyl groups in proteins as evaluated by residual dipolar couplings
复制标题
通过残余偶极耦合评估氘化对蛋白质中甲基的一些结构参数的影响
DOI：
10.1023/a:1015368803552
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发表时间：
2002
影响因子：
2.7
通讯作者：
L. Kay
中科院分区：
文献类型：
--
作者：
A. Mittermaier;L. Kay
在一个15N， 13C， ~ 50% 2H标记的胃链球菌蛋白L的B1免疫球蛋白结合域的样品中，测量了一个键甲基1H-13C和13Cmethyl -13C的标量偶极偶联和残余偶极偶联，以研究氘取代反应中甲基结构的变化。单键甲基1H-13C和13Cmethyl -13C的标量偶联常数随氘含量的增加而略有降低。先前的研究表明，甲基上的1H-13C偶联对电子结构非常敏感，偶联值随氘度的变化而降低，与剩余的H-C键的轻微延长一致。CH3、CH2D和CH3、CHD2同位素体的HmethylCmethylC角变化较小，平均差异分别为0.3±0.1°和0.4±0.2°。甲基几何知识是从涉及这些基团的自旋弛豫研究中提取准确动力学参数的先决条件。
One bond methyl 1H-13C and 13Cmethyl−13C scalar and residual dipolar couplings have been measured at sites in an 15N, 13C, ∼ 50% 2H labeled sample of the B1 immunoglobulin binding domain of peptostreptococcal protein L to investigate changes in the structure of methyl groups in response to deuterium substitution. Both one bond methyl 1H-13C and 13Cmethyl−13C scalar coupling constants have been found to decrease slightly with increasing deuterium content. Previous studies have shown that 1H-13C couplings in methyl groups are exquisitely sensitive to electronic structure, with decreases in coupling values as a function of deuteration consistent with a slight lengthening of the remaining H-C bonds. Changes in the HmethylCmethylC angle are found to be small, with average differences on the order of 0.3 ± 0.1° and 0.4 ± 0.2° between CH3, CH2D and CH3, CHD2 isotopomers, respectively. Knowledge of methyl geometry is a prerequisite for the extraction of accurate dynamics parameters from spin relaxation studies involving these groups.
影响因子：
2.9
作者：
NICHOLSON, LK;KAY, LE;TORCHIA, DA
通讯作者：
TORCHIA, DA