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Protein tolerance to random circular permutation correlates with thermostability and local energetics of residue-residue contacts
Adenylate kinase (AK) orthologs with a range of thermostabilities were subjected to random circular permutation, and deep mutational scanning was used to evaluate where new protein termini were nondisruptive to activity. The fraction of circularly permuted variants that retained function in each lib...
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| Publicado no: | Protein Eng Des Sel |
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| Main Authors: | , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Oxford University Press
2019
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7462040/ https://ncbi.nlm.nih.gov/pubmed/32626892 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/protein/gzaa012 |
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