Journal:JBSD:22
From Proteopedia
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<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 | + | 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. |
| - | 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
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- ↑ 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.
