Energetics of repacking a protein interior.
To test whether interactions in the hydrophobic core of a protein can be adequately modeled based on the properties of a liquid hydrocarbon, we measured the unfolding free energies of the wild-type bacteriophage f1 gene V protein and 29 mutants with apolar substitutions at positions 35 and 47. Stabi...
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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
1991
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC51093/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2000379/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.88.5.1706 |
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