Physical organic chemistry in the brain

Abstract

A new tool for precise structural modification of ion channel proteins - the in vivo nonsense suppression technique for incorporating unnatural amino acids - has been developed. This new tool allows the kind of systematic structure-function correlation studies that are commonly employed in physical organic chemistry to be applied to the important proteins of molecular neurobiology. In particular, the method has been applied to the nicotinic acetylcholine receptor, The differing roles of the numerous aromatic amino acids present at the agonist binding site can be distinguished. In addition, high precision studies of the ion channel region have produced new insights into the channel gating mechanism.