The sequences of small proteins are not extensively optimized for rapid folding by natural selection
The thermodynamic stabilities of small protein domains are clearly subject to natural selection, but it is less clear whether the rapid folding rates typically observed for such proteins are consequences of direct evolutionary optimization or reflect intrinsic physical properties of the polypeptide...
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| Publicado no: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
1998
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC20199/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9560214/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.95.9.4982 |
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