PROTEIN FOLDS IN CHANNEL STRUCTURE

Advances have been made during the past year in our understanding of t he structural basis of channel-protein function. With the convergence of conceptual and technical breakthroughs, we stand at the threshold o f an exciting phase in the analysis of membrane proteins with the same molecular detail that used to be the exclusive domain of aqueous solu ble proteins. The provocative prospect of establishing the occurrence of minimum units of structure with specific functional attributes may provide a realistic pathway towards understanding the fundamental prin ciples underlying the sequence-structure determinism.