...
首页> 外文期刊>Electrophoresis: The Official Journal of the International Electrophoresis Society >CONVERGENCE OF AMINO ACID COMPOSITIONS OF CERTAIN GROUPS OF PROTEINS AIDS IN THEIR IDENTIFICATION ON TWO-DIMENSIONAL ELECTROPHORESIS GELS
【24h】

CONVERGENCE OF AMINO ACID COMPOSITIONS OF CERTAIN GROUPS OF PROTEINS AIDS IN THEIR IDENTIFICATION ON TWO-DIMENSIONAL ELECTROPHORESIS GELS

机译:二维电泳凝胶鉴定中某些蛋白质艾滋病的氨基酸组成的收敛性

获取原文
获取原文并翻译 | 示例
   

获取外文期刊封面封底 >>

       

摘要

'The amino acid composition (AAC) versus the protein identity (PI) method was used for establishment of the identities of proteins from bovine brain and kidneys which were prefractionated on a CM52 cation exchanger and by preparative flat-bed isoelectric focusing. Established identities of proteins whose AACs converge with those of other members of their proper superfamily are reliable. Groups of convergent AACs can be extracted from protein databases using the standard root-mean-square rule (Rmsd) with measures the difference between the AAC of chosen protein versus those in the database. Convergence of AACs of proteins is dependent on several factors such as the upper limit of Rmsd, the limits of variations of molecular mass (m) and isoelectric point (pr), the number of proteins with similar AACs present in protein databases, and the domain structure of proteins. AACs of many proteins remain unique if the Rmsd is maintained within 1.5-1.0 with m +/- 3kDA and pI +/- 4. Certain groups of multidomain proteins have quasi-unique AACs only if the Rmsd is restrained to a value within 1.0 and 0.7. Convergence of AACs of certain groups of proteins may indicate that a common biological function exists for some members of each group. The AAC-PI method may become an additional search tool for protein functions. [References: 27]
机译:氨基酸组成(AAC)与蛋白质同一性(PI)方法用于确定来自牛脑和肾脏的蛋白质的同一性,这些蛋白质在CM52阳离子交换剂上进行分馏并通过制备式平板等电聚焦进行了鉴定。其AAC与其适当超家族其他成员的AAC融合的蛋白质的确定身份是可靠的。可以使用标准均方根规则(Rmsd)从蛋白质数据库中提取收敛的AAC组,并测量所选蛋白质与数据库中AAC之间的差异。蛋白质AAC的收敛性取决于多个因素,例如Rmsd的上限,分子量(m)和等电点(pr)的变化极限,蛋白质数据库中存在具有相似AAC的蛋白质数量以及结构域蛋白质的结构。如果Rmsd保持在1.5-1.0之间,且m +/- 3kDA和pI +/- 4,则许多蛋白质的AAC保持唯一。只有当Rmsd限制在1.0和1.0之间时,某些多域蛋白组才具有准唯一AAC。 0.7。某些蛋白质组的AAC趋同可能表明每组某些成员存在共同的生物学功能。 AAC-PI方法可能成为蛋白质功能的另一种搜索工具。 [参考:27]

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
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