C-H...π interactions are known to be important contributors to protein stability. In this study, we have analyzed the influence of C-H...π interactions on the structural stability of membrane proteins. In the data set, a total of 408 C-H....π interactions were observed. The most prominent representatives are the interactions between aromatic C-H donor groups and aromatic π acceptors. Ninety four percent of the C-H....π interactions between side chain to side chain and remaining six percent of the C-H....π interactions were observed between sidechain to side-chain five-membered aromatic ring. Long-range C-H....π interactions are the predominant type of interactions in membrane proteins data set. The secondary structure preference, solvent accessibility and stabilization centers of C-H....π interacting residues were estimated. Moreover, the study shows that 72% of the donor residues and 68% of the acceptor residues are highly conserved.. It is concluded that the C-H....π interaction can, indeed, be categorized as a true stabilizing force in membrane proteins.