Codon Harmonization of a Kir3.1-KirBac1.3 Chimera for Structural Study Optimization.

ABSTRACT: The expression of functional, folded, and isotopically enriched membrane proteins is an enduring bottleneck for nuclear magnetic resonance (NMR) studies. Indeed, historically, protein yield optimization has been insufficient to allow NMR analysis of many complex Eukaryotic membrane proteins. However, recent work has found that manipulation of plasmid codons improves the odds of successful NMR-friendly protein production. In the last decade, numerous studies showed that matching codon usage patterns in recombinant gene sequences to those in the native sequence is positively correlated with increased protein yield. This phenomenon, dubbed codon harmonization, may be a powerful tool in optimizing recombinant expression of difficult-to-produce membrane proteins for structural studies. Here, we

SUBMITTER: van Aalst E 

PROVIDER: S-EPMC7175280 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature