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Article

Protein tolerance to random circular permutation correlates with thermostability and local energetics of residue-residue contacts.

Protein engineering, design & selection : PEDS - 31 Dec 2019

Atkinson Joshua T, Jones Alicia M, Nanda Vikas, Silberg Jonathan J

Abstract excerpt

Adenylate kinase (AK) orthologs with a range of thermostabilities were subjected to random circular permutation, and deep mutational scanning was used to evaluate where new protein termini were nondisruptive to activity. The fraction of circularly permuted variants that retained function in each library correlated with AK thermostability. In addition, analysis of the positional tolerance to new termini, which...

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PMID: 32626892
DOI: 10.1093/protein/gzaa012
PMCID: PMC7462040

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