Dr. Conti-Tronconi studies the relationship between the molecular structure and function of the nicotinic receptor, a membrane protein which recognizes and binds acetylcholine. Acetylcholine is an ubiquitous neurotransmitter, which mediates transmission of commands between nerve cells and between neurons and effector cells, such as muscle. For this reason, Dr. Conti-Tronconi's research has both theoretical and practical implications. She has developed a technique to define separate regions of the nicotinic receptor, using antibodies raised against fragments of the receptor molecule, which are isolated by reacting the receptors with naturally occurring poisons. When these antibodies react with native receptors they disturb the receptor's function. These data are then used to construct a steric and functional model of the molecule. Dr. Conti-Tronconi intends to exploit fully the advantages of this technical approach by systematically altering the amino acids sequence in separate fragments of the nicotinic receptor already recognized; the functional effects of these modifications will be assessed by testing the ability of the altered segment to bind to poisons as well as to antibodies raised against intact fragments. Dr. Conti-Tronconi also intends to complement these studies by obtaining maps of nicotinic receptor fragments by Nuclear Magnetic Resonance and by X-ray diffraction. The most ambitious goal of the research is to define the structure of the receptor which determines the selectivity of this membrane protein to ion flow. These same techniques, once proven and refined in studying the nicotinic receptors, can be applied in the future to the elucidation of other functional structure of other receptors' molecules.
