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Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant
Our goal was to compute a stable, full-sequence design of the Drosophila melanogaster engrailed homeodomain. Thermal and chemical denaturation data indicated the design was significantly more stable than was the wild-type protein. The data were also nearly identical to those for a similar, later ful...
Tallennettuna:
| Päätekijät: | , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Cold Spring Harbor Laboratory Press
2005
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2253454/ https://ncbi.nlm.nih.gov/pubmed/15741348 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.041277305 |
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