Molecular dynamics of an extremely thermophilic ribose binding protein

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

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


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.

Original languageEnglish
Pages (from-to)606-610
Number of pages5
JournalActa Chimica Sinica
Issue number5
StatePublished - 14 Mar 2012
Externally publishedYes


  • Extremely hemophilic
  • Flexibility
  • Intramolecular concerted motions
  • Molecular dynamics
  • TteRBP (Thermoanaerobacter tengcongensis ribose binding protein)


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