摘要
采用分子动力学模拟方法研究极端嗜热性核糖结合蛋白(tteRBP)的嗜热机理.在常温(300 K)和最佳活性温度(375 K)时,分别对tteRBP分子进行动力学模拟,结果表明,整体分子均保持结构稳定,但分子内部的协调运动不同.在375 K时蛋白整体柔性显著提高,使分子能够局部调整构象以适应极端高温.蛋白结构变化的分析也确认了高温时构象局部微调对蛋白极端高温稳定性的关键作用.
Molecular dynamics simulations for extremely thermophilic protein thermoanaerobacter teng- congensis ribose binding protein （tteRBP） were performed to investigate the thermophilic mechanism of the protein. The comparative analysis of molecular trajectories of room temperature （300 K） and optimal activity temperature （375 K） shows that the protein conformations are stably maintained, but the concerted motions are different. The flexibility of the protein at 375 K significantly increases, so the protein can adjust the local conformation to adapt to extreme temperature. The analysis of the changes in protein structure confirmed that the local conformation adjustment at 375 K olavs a key role on the extreme hizh temoerature stability.
出处
《化学学报》
SCIE
CAS
CSCD
北大核心
2012年第5期606-610,共5页
Acta Chimica Sinica
