...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >X-ray crystallographic studies on the hydrogenisotope effects of green fluorescent protein atsub-angstrom resolutions
【24h】

X-ray crystallographic studies on the hydrogenisotope effects of green fluorescent protein atsub-angstrom resolutions

机译：x射线晶体研究hydrogenisotope绿色荧光的影响蛋白质atsub-angstrom决议

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Hydrogen atoms are critical to the nature and properties of proteins, and thusdeuteration has the potential to influence protein function. In fact, it has beenreported that some deuterated proteins show different physical and chemicalproperties to their protiated counterparts. Consequently, it is important toinvestigate protonation states around the active site when using deuteratedproteins. Here, hydrogen isotope effects on the S65T/F99S/M153T/V163Avariant of green fluorescent protein (GFP), in which the deprotonated B formis dominant at pH 8.5, were investigated. The pH/pD dependence of theabsorption and fluorescence spectra indicates that the protonation state of thechromophore is the same in protiated GFP in H_2O and protiated GFP in D_2O atpH/pD 8.5, while the pK_a of the chromophore became higher in D_2O. Indeed,X-ray crystallographic analyses at sub-angstrom resolution revealed noapparent changes in the protonation state of the chromophore between thetwo samples. However, detailed comparisons of the hydrogen OMIT mapsrevealed that the protonation state of His148 in the vicinity of the chromophorediffered between the two samples. This indicates that protonation states aroundthe active site should be carefully adjusted to be the same as those of theprotiated protein when neutron crystallographic analyses of proteins areperformed.
机译：的性质和氢原子是至关重要的蛋白质的性质,thusdeuteration可能影响蛋白质功能。事实上,beenreported一些氘显示不同的物理和蛋白质chemicalproperties他们protiated同行。调查周围的质子化作用状态使用deuteratedproteins时活性部位。氢同位素的影响S65T / F99S / M153T / V163Avariant绿色荧光蛋白(GFP), formis deprotonated B在pH值为8.5,占主导地位的调查。依赖theabsorption和荧光光谱表明,质子化作用的状态thechromophore protiated GFP在相同H_2O和protiated GFP D_2O atpH / pD 8.5,发色团的pK_a变得更高D_2O。sub-angstrom分辨率显示noapparent的质子化作用状态的变化发色团之间的两个样本。氢的详细比较省略掉mapsrevealed His148的质子化作用状态附近的chromophorediffered在两个样品之间。质子化作用的州就在活性部位小心地调整的相同theprotiated蛋白质时,中子晶体分析的蛋白质areperformed。

著录项

相似文献

  • 外文文献
  • 中文文献
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号