The approach to probing the sequence-structure relationship of ion-cha
nnel proteins using small peptides stems from the abundance of sequenc
e information and the virtual absence of structures at atomic resoluti
on. It is anticipated that model peptides may fold predictably into st
able structures and reproduce functional properties of specific protei
ns. Model peptides are well suited to the application of NMR methods t
o determine protein structure in a membrane environment or to high-res
olution X-ray diffraction analysis. It is timely to ask what we have l
earned through this strategy and where it may lead in our quest to und
erstand the sequence-structure determinism.