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Two carbohydrate mutants of human choriogonadotropin alpha lacking N-glycosyl chains at alpha52Asn and alpha78Asn were constructed. Circular dichroism of the two constructs revealed that the the absence of carbohydrate at the alpha52Asn resulted in conformational changes in the mutant causing the loss of signal transduction function. The function of alpha52Asn was the maintenance of the conformational integrity of the heterodimer rather than direct influence in the receptor binding.

Incorporation of taxol into liposomes results in the penetration of taxol in the acyl chain domain of the dipalmitoylphosphatidylcholine (DPPC) bilayer, which changes the physical properties of artificial and biological membranes. Studies of the conformation of taxol and its interaction with DPPC liposomes reveal that the conformation in DPPC membranes is similar to that in nonpolar solvents such as chloroform. The insertion of taxol into the bilayer disturbs the hydrocarbon chain formation, widening the DPPC phase transition.