The production of recombinant inner membrane proteins utilising the T7 system often results in low yields due to poor expression levels. Despite the creation of E. coli membrane protein expression strains such as C41(DE3), some membrane proteins are still poorly expressed. It has been hypothesised that this poor expression is due to cellular stress responses caused by the saturation of the Sec translocon. This results in the formation of inclusion bodies, poor ATP production, induction of the heat shock response, and poor cellular growth, all of which limit the protein yields obtained from over-expression. It has been proposed that manipulating the translocation machinery by increasing the expression of its components could increase the translocational capacity of the cell and, thus, prevent the saturation of the Sec machinery. This project assesses this proposition using a genome-scale metabolic model of metabolism, protein production and translation, to predict/identify the limiting translocation components and the effects of incorporating artificial operons to supplement the expression of these components on the growth/yields obtained from recombinant inner membrane protein production. It was found that requirement of a Sec-mediated translocation reaction greatly impairs cell growth and that the co-expression of specific Sec components can compensate for this defect. Future research shall investigate and validate these interactions in vivo.