Journal:JBSD:22
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
<StructureSection load='' size='450' side='right' scene='' caption=''> | <StructureSection load='' size='450' side='right' scene='' caption=''> | ||
=== Molecular dynamics simulations of the thermal stability of tteRBP and ecRBP === | === Molecular dynamics simulations of the thermal stability of tteRBP and ecRBP === | ||
| - | <big>Xi | + | <big>Xian-li Feng, Xi Zhao, Hui Yu, Tie-dong Sun, Xu-ri Huang</big> <ref>REF</ref> |
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | + | The backbone structure of tteRBP (optimal activity temperature is 375 K) and ecRBP (optimal activity temperature is 329K) is very similar, but significantly | |
| + | different in thermal stability. This is particularly attractive us. | ||
| + | In order to investigate the thermal stability of tteRBP and ecRBP, we found the backboneuse flexibility and verify the side-chain interactions both are the key factors to maintain thermal stability of the two proteins by molecular dynamics (MD)simulation method. | ||
</StructureSection> | </StructureSection> | ||
<references/> | <references/> | ||
__NOEDITSECTION__ | __NOEDITSECTION__ | ||
Revision as of 11:17, 5 September 2012
| |||||||||||
- ↑ REF
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
