As an approach to investigate the molecular mechanism of in vivo protein folding and the role of translation kinetics on specific folding pathways, we
made codon substitutions in the EgFABP1 (Echinococcus granulosus fatty acid binding protein1) gene that replaced five minor codons with their
synonymous major ones. The altered region corresponds to a turn between two short alpha helices. One of the silent mutations of EgFABP1 markedly
decreased the solubility of the protein when expressed in Escherichia coli. Expression of this protein also caused strong activation of a reporter
gene designed to detect misfolded proteins, suggesting that the turn region seems to have special translation kinetic requirements that ensure proper
folding of the protein. Our results highlight the importance of codon usage in the in vivo protein folding.
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