Article
Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification.
Protein science : a publication of the Protein Society - 1 Feb 2001
Ross S A, Sarisky C A, Su A, Mayo S L
Abstract excerpt
The solution structures of two computationally designed core variants of the beta 1 domain of streptococcal protein G (G beta 1) 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 variant has mutations at three of 10 core positions and corresponds to minimal perturbations of the native G...
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