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Designed protein G core variants fold to native-like structures: Sequence selection by ORBIT tolerates variation in backbone specification
The solution structures of two computationally designed core variants of the β1 domain of streptococcal protein G (Gβ1) were solved by (1)H NMR methods to assess the robustness of amino acid sequence selection by the ORBIT protein design package under changes in protein backbone specification. One v...
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| Hauptverfasser: | , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
Cold Spring Harbor Laboratory Press
2001
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2373933/ https://ncbi.nlm.nih.gov/pubmed/11266631 |
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