Acta Chimica Sinica ›› 2012, Vol. 0 ›› Issue (05): 606-610 .DOI: 10.6023/A1107031 Previous Articles     Next Articles

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冯献礼, 赵熹, 于辉, 王乙博, 孙铁东, 黄旭日   

  1. 吉林大学理论化学研究所理论化学计算国家重点实验室 长春 130023
  • 投稿日期:2011-07-03 修回日期:2011-11-20 发布日期:2011-12-06
  • 通讯作者: 黄旭日

Molecular Dynamics of an Extremely Thermophilic Ribose Binding Protein

Feng Xianli, Zhao Xi, Yu Hui, Wang Yibo, Sun Tiedong, Huang Xuri   

  1. State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130023
  • Received:2011-07-03 Revised:2011-11-20 Published:2011-12-06

Molecular dynamics simulations for extremely thermophilic protein thermoanaerobacter tengcongensis 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 plays a key role on the extreme high temperature stability.

Key words: tteRBP (Thermoanaerobacter tengcongensis ribose binding protein), molecular dynamics, intramolecular concerted motions, flexibility, extremely hemophilic