氢键与蛋白质耐热性关系的研究

挑选了NCBI COG数据库中具有全基因组的单细胞微生物,选择其中已知三维结构的蛋白质作为研究对象,通过HB- Plus3．0计算出氢键数目并用Perl编程将氢键分类,研究了不同类型的氢键对蛋白质耐热性的影响。结果表明:随着耐热性增高,古细菌类蛋白质中氢键总含量、主链-主链氢键含量,以及非电荷-非电荷氢键含量有显著降低;细菌类蛋白质带电荷-带电荷氢键含量显著增加,而非电荷-非电荷氢键含量显著降低。它们唯一的共同点都是避免在耐热蛋白质中形成非电荷-非电荷氢键。

The study on the relationship between hydrogen bond and protein thermostability

We selected all complete genome unicellular microorganisms from NCBI COG database, and collected all proteins whose three-dimensional structure had been measured to study the influence of different types hydrogen bond on protein thermostability (the proteins had been classified to bacterial proteins and archaeal proteins). We used HBPlus3.0 to calculate the hydrogen bond numbers and the hydrogen bond was classified by Perl program. The results show: when protein thermostability increased, all the hydrogen bond numbers in protein, main chain-main chain hydrogen bond numbers and uncharged-uncharged hydrogen bond numbers decreased dramatically in archaeal protein; for bacterial protein, the charged-charged hydrogen bond numbers increased dramtically, while uncharged-uncharged hydrogen bond numbers decreased dramtically. The common ground is that they avoid to form uncharged-uncharged hydrogen bond in thermophilic proteins.