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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: Schweiker, Katrina L., Zarrine-Afsar, Arash, Davidson, Alan R., Makhatadze, George I.
Format: Artigo
Idioma:Inglês
Publicat: Cold Spring Harbor Laboratory Press 2007
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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