Stability of therapeutic proteins contributes significantly towards the discovery of new drug molecules. We have investigated the role of C-H...O interactions on the structural stability of therapeutic proteins. In our study we have analyzed the interactions in a set of 48 therapeutic proteins. A total of 1099 interactions were observed with an average of 23 C-H...O interactions per therapeutic protein. The analysis of the position of interacting residues in therapeutic proteins showed that C-H...O interactions are mainly formed by long range contacts. Phe has the highest occurrence among the donor residues while Glu has the highest occurrence among the acceptor residues. The C-H...O interaction residues involved in these proteins were found highly conserved with more than 50% of the interacting residues either as a donor or as a acceptor having conservation score of ≥6. The results obtained in the present study should be useful in understanding the contribution of C-H...O interactions towards the structural stability and specificity of therapeutic proteins.