Protein thermal stability, hydrogen bonds, and ion pairs
Protein thermal stability, hydrogen bonds, and ion pairs
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DOI：
10.1006/jmbi.1997.1042
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发表时间：
1997-06-20
影响因子：
5.6
通讯作者：
Argos, P
中科院分区：
文献类型：
--
作者：
Vogt, G;Woell, S;Argos, P
学术界和工业界的研究人员都对理解提高蛋白质热稳定性的机制表现出浓厚的兴趣。对于稳定性的提高，人们已经提出了许多不同的结构原理。在此，通过比较16个具有不同热稳定性的蛋白质家族各自的极性原子表面积分数以及明确的蛋白质原子之间氢键和盐键的数量和类型，对它们进行了理论研究。在超过80%的家族中，发现家族成员的热稳定性与氢键数量的增加以及极性表面分数的增加之间存在相关性，这导致了与水的氢键密度增加。因此，氢键的增加可能为蛋白质的热稳定性提供最普遍的解释。在三分之二接受测试的家族中，还发现离子对的数量随着热稳定性的增加而增加；然而，它们增加的速率仅约为蛋白质原子之间内部氢键增加速率的六分之一。还研究了在工程改造中提高稳定性有用的优先残基交换和表面原子类型。(C) 1997学术出版社有限公司
Researchers in both academia and industry have expressed strong interest in comprehending the mechanisms responsible for enhancing the thermostability of proteins. Many and different structural principles have been postulated for the increased stability. Here, 16 families of proteins with different thermal stability were theoretically examined by comparing their respective fractional polar atom surface areas and the number and type of hydrogen bonds and salt links between explicit protein atoms. In over 80% of the families, correlations were found between the thermostability of the familial members and an increase in the number of hydrogen bonds as well as an increase in the fractional polar surface which results in added hydrogen bonding density to water. Thus increased hydrogen bonding may provide the most general explanation for thermal stability in proteins. The number of ion pairs was also found to increase with thermal stability in two-thirds of the families tested; however, their rate of addition was only about one-sixth that for internal hydrogen bonds amongst the-protein atoms. The preferred residue exchanges and surface atom types useful in engineering enhanced stability were also examined. (C) 1997 Academic Press Limited.