Cyclooxygenase-2 (COX-2) and microsomal prostaglandin E synthase-1 (mPGES-1) structures were studied using both photo-methionine (photo-activatable) and bifunctional cross linkers. Photo-methionine used in COX-2 had shown just as the bifunctional cross-linker that there was a dimeric structure which this was consistent with the crystal structure of the enzyme. In mPGES-1, the human cells (A549) had been treated with disuccinimidyl suberate (chemical cross-linker) had yielded a dimer of 33kDa and a trimer of 45kDa while it was treated with photo-methionine had yielded a dimer of the same molecular weight (33kDa) and two putative trimers (50kDa and 55kDa). Once a mPGES-1 inhibitor (MF63) was introduced; this had inhibited the formation of the 50kDa and 55kDa complexes. The dimer and trimer yielded by the chemical cross-linker was not affected by the inhibitor. Yet, photo-methionine nor disuccinimidyl suberate had not shown any protein-protein interactions between COX-2 and mPGES-1 and this could be due to various reasons. For photo-methionine; one could be due to the low incorporation at this time as it was 0.7%. So, for mPGES-1; this has 152 amino acids so only one photo-methionine would be incorporated per monomer. That also means not one specific methionine would be replaced so that results in a heterogeneous population of mPGES-1 resulting in different cross-linking. Even though it did not show any protein-protein interactions, it could be used to detect inhibitor-induced protein conformational changes in the cell membranes on top of determining oligomeric structures.