Isoelectric points of multi-domain proteins
Isoelectric points of multi-domain proteins
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DOI：
10.6026/97320630002101
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发表时间：
2007-01-01
期刊：
影响因子：
1.9
通讯作者：
Carugo, Oliviero
中科院分区：
文献类型：
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作者：
Carugo, Oliviero
尽管蛋白质等电点的分布是多峰的，但随着蛋白质尺寸的增加，大蛋白质的等电点比小蛋白质的等电点变化更小，它们的等电点往往收敛到一个唯一的值，接近蛋白质发挥功能的环境的pH值。这项研究表明，包含多个结构域的大蛋白的等电点确实比包含单个结构域的小蛋白的等电点变化小。然而，包含在大蛋白质中的单个结构域的等电点的分布类似于包含单个结构域的小蛋白质的分布。因此，即使大蛋白质的等电点非常接近它们执行其功能的环境的pH值，它们也是可以溶解的，因为它们可以包含几个结构域，每个结构域的静电特性反映了小蛋白质的静电特性。
Although the distribution of protein isoelectric points is multi-modal, large proteins show isoelectric points less variable than small proteins and their isoelectric points tend to converge to a unique value, close to the pH of the milieu in which the proteins are functional, as far as the protein dimension increases. This study demonstrates that large proteins, which contain more than a single domain, do have isoelectric points less variable than small proteins, which contains a single domain. However, the distribution of the isoelectric points of the single domains, contained in large proteins, resembles that of small proteins, which contain a single domain. Thus, large proteins can be soluble even if their pI is very close to the pH of the milieu, in which they perform their function, since they can contain several domains, the electrostatic properties of each of which mirror those of small proteins.