Peptide-based approaches to protein structure within membranes have proven
enormously valuable. When one focusses on the detailed manner through which
membrane proteins actually traverse the cell bilayer, a simple observation
emerges: helical peptide segments of 20 amino acids each constitute the on
ly tangible connection between the inside and outside of the cell. Thus, a
major step towards understanding the key relationships between biological f
unction and membrane protein structure can be taken through characterizatio
n, by composition, sequence, chain length, hydrophobicity and conformation,
of hydrophobic peptides designed as mimics of transmembrane segments.