Codon usage bias is a universal feature of eukaryotic and prokaryotic genomes. It has been proposed that synonymous codons can affect the velocity of protein translation and as a consequence translation accuracy and protein folding. Here we used small K+ channels to examine the impact of codon usage on basic parameters of ion channel function. The model channel KcvPBCV1 was therefore expressed in a cell-free translation system and reconstituted in planar lipid bilayers for single channel recordings. We find that preferred codons enhance the rate of translation elongation. This has no impact on the unitary conductance of the channel but eliminates one voltage dependent gating component. The data underscore that the same amino acid sequence can generate proteins with distinctly different functional features. The dynamics of protein synthesis hence provides an additional layer for the modulation of structure/function correlates in ion channels. This could be important for an understanding of so called “silent mutations”, which are so far generally ignored in the context of an analysis of channelopathies.