RELATIONSHIP OF PROTEIN FLEXIBILITY TO THERMOSTABILITY
RELATIONSHIP OF PROTEIN FLEXIBILITY TO THERMOSTABILITY
复制标题
DOI：
10.1093/protein/1.6.477
复制
发表时间：
1987-12-01
期刊：
影响因子：
--
通讯作者：
VIHINEN, M
中科院分区：
文献类型：
--
作者：
VIHINEN, M
蛋白质的热稳定性来自于几种力的同时作用，这实际上导致多肽链的柔性降低。这是验证的灵活性指数，这是来自归一化的B值的个别氨基酸在几个精致的三维结构。柔韧性指数表明，当热稳定性增加时，整体柔韧性降低。蛋白质分子需要柔性和刚性才能发挥作用，但最佳温度和稳定性越高，补偿增加的热波动所需的结构就越刚性。表现相同催化活性的蛋白质在其最适温度下的柔韧性似乎大致相同，但更刚性的热稳定蛋白质在更高温度下达到不耐热蛋白质的柔韧性。在一些蛋白质如变构酶中，一些局部柔性位点是高度保守的。还讨论了蛋白质的整体稳定性的灵活性降低的相关性。柔性指数和分布可用于通过定点诱变设计更稳定的蛋白质。
Thermostability of proteins arises from the simultaneous effect of several forces, which in fact lead to decreased flexibility of the polypeptide chain. This is verified by flexibility indices, which are derived from normalized B-values of individual amino acids in several refined three-dimensional structures. Flexibility indices show that overall flexibility is reduced when thermostability is increaed. Protein molecules require both flexibility and rigidity to function, but the higher the temperature optimum and stability the more rigid is the structure needed to compensate for increased thermal fluctuations. Flexibilities of proteins performing the same catalytic activity seem to be about the same at their temperature optima, but the more rigid thermostable proteins reach the flexibility of thermolabile proteins at higher temperatures. In several proteins such as allosteric enzymes, some local sites of flexibility are highly conserved. The relevance of reduced flexibility to overall stability of proteins is also discussed. Flexibility indices and profiles can be used in the design of more stable proteins by site-directed mutagenesis.