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Abstract

Despite their functional relevance, little is known about the structures of the strongly hydrophobic transmembrane segments of integral membrane proteins such as the inhibitory glycine receptor [l].This receptor belongs to a class of topologically simple membrane proteins. It forms an anion channel due to the supramolecular association of five monomers, each consisting of four putative transmembrane segments Ml, M2, M3 and M4. M2 is unusually polar and thus thought to be involved in anion conduction. In order to span a membrane, the polar M2 would have to be stabilized by interacting with strongly nonpolar segments. Because it is difficult to crystallize membrane proteins for carrying out high resolution crystal structure determinations, alternative approaches employing for example spectroscopic methods need to be developed to obtain informations about structural features such as of single transmembrane segments.