Molecular Dynamics of an Extremely Thermophilic Ribose Binding Protein

作者：Feng Xianli^*; Zhao Xi; Yu Hui; Wang Yibo; Sun Tiedong; Huang Xuri

来源：Acta Chimica Sinica, 2012, 70(5): 606-610.

DOI：10.6023/A1107031

• tteRBP (Thermoanaerobacter tengcongensis ribose binding protein)
• molecular dynamics
• intramolecular concerted motions
• flexibility
• extremely hemophilic

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.

• 出版日期2012-3-14
• 单位吉林大学