- Abstract:
-
The effects of temperature and urea denaturation (6M urea) on the dominant structures of the 20-residue Trp-cage mini-protein TC5b are investigated by molecular dynamics simulations of the protein at different temperatures in aqueous and in 6M urea solution using explicit solvent degrees of freedom and the GROMOS force-field parameter set 45A3. In aqueous solution at 278 K, TC5b is stable throughout the 20 ns of MD simulation and the trajectory structures largely agree with the NMR-NOE atom-a...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1002/pro.223
-
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- Journal:
- Protein science : a publication of the Protein Society
- Volume:
- 18
- Issue:
- 10
- Pages:
- 2090-2099
- Publication date:
- 2009-10-05
- DOI:
- EISSN:
-
1469-896X
- ISSN:
-
0961-8368
- URN:
-
uuid:1e77c355-dc00-44e6-8a00-09f97a65b6c9
- Source identifiers:
-
34844
- Local pid:
- pubs:34844
- Language:
- English
- Keywords:
- Copyright date:
- 2009
Journal article
Temperature and urea induced denaturation of the TRP-cage mini protein TC5b: A simulation study consistent with experimental observations.
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