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Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins
We compared folding properties of designed protein Top7 and natural protein S6 by using coarse-grained chain models with a mainly native-centric construct that accounted also for nonnative hydrophobic interactions and desolvation barriers. Top7 and S6 have similar secondary structure elements and ar...
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| Hlavní autoři: | , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
2010
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2840274/ https://ncbi.nlm.nih.gov/pubmed/20133730 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0911844107 |
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