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The structure of a thermophilic kinase shapes fitness upon random circular permutation
Proteins can be engineered for synthetic biology through circular permutation, a sequence rearrangement where native protein termini become linked and new termini are created elsewhere through backbone fission. However, it remains challenging to anticipate a protein’s functional tolerance to circula...
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| Publicado en: | ACS Synth Biol |
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| Autores principales: | , , , , , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
2016
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5122316/ https://ncbi.nlm.nih.gov/pubmed/26976658 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acssynbio.5b00305 |
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