Thermal stability and kinetic constants for 129 variants of a family 1 glycoside hydrolase reveal that enzyme activity and stability can be separately designed.
Accurate modeling of enzyme activity and stability is an important goal of the protein engineering community. However, studies seeking to evaluate current progress are limited by small data sets of quantitative kinetic constants and thermal stability measurements. Here, we report quantitative measur...
Guardado en:
| Autores principales: | , , , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
Public Library of Science (PLoS)
2017-01-01
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| Colección: | PLoS ONE |
| Acceso en línea: | http://europepmc.org/articles/PMC5439667?pdf=render |
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