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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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Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς: Ross, Scott A., Sarisky, Catherine A., Su, Alyce, Mayo, Stephen L.
Μορφή: Artigo
Γλώσσα:Inglês
Έκδοση: Cold Spring Harbor Laboratory Press 2001
Θέματα:
Διαθέσιμο Online:https://ncbi.nlm.nih.gov/pmc/articles/PMC2373933/
https://ncbi.nlm.nih.gov/pubmed/11266631
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