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Computational design of the Fyn SH3 domain with increased stability through optimization of surface charge–charge interactions
Computational design of surface charge–charge interactions has been demonstrated to be an effective way to increase both the thermostability and the stability of proteins. To test the robustness of this approach for proteins with predominantly β-sheet secondary structure, the chicken isoform of the...
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| Autors principals: | , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Cold Spring Harbor Laboratory Press
2007
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2222822/ https://ncbi.nlm.nih.gov/pubmed/18029422 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.073091607 |
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