دورية
The Mechanism of TC230′s Thermostability: A Molecular Dynamics Simulation Study
| العنوان: | The Mechanism of TC230′s Thermostability: A Molecular Dynamics Simulation Study |
|---|---|
| المؤلفون: | Guo, Zhi, Xu, Li-Na, Zhou, Lin-Xiang |
| المصدر: | Journal of Biomolecular Structure and Dynamics; June 2006, Vol. 23 Issue: 6 p603-611, 9p |
| مستخلص: | AbstractThe quasielastic neutron scattering index β and the modulus of a protein's quasi-electric dipole moment were utilized to quantitate the thermostability of wildtype TC230 and its mutants. Charged residues Arg314, Glu246, Glu291, and some prolines near the C-terminus of the sequence (Pro228, Pro296, and Pro308) were identified to be critical for the thermostability of wildtype TC230 according to these two criteria. By analyzing the molecular conformation changes during the simulation, it was demonstrated how the mutant P228S was destabilized by disrupting two salt-bridges Asp1160Dl-Lys215N and Glu2100El-Lys217N at an adjacent β-turn. The destabilization of P296S also shown to be intimate correlated with the break down of ion pair Lysl88N-Glu2910El. The sensitivity of its electrostatic network to the local structure is an important feature. It reveals that the ‘proline effect’ and electrostatic interactions together influences the thermostability of TC230 a lot. |
| قاعدة البيانات: | Supplemental Index |
PDF full text from Publisher 
Full Text Finder | تدمد: | 07391102 15380254 |
|---|---|
| DOI: | 10.1080/07391102.2006.10507085 |