Transmembrane helices from crystallographically determined structures were
analyzed to determine the distribution of side chains inside and outside he
lix-helix interfaces. Two structural characteristics were explored: (1) the
number of atoms outside the interfaces that belong to the side chains with
the C-alpha atoms inside the interfaces, as well as the opposite, inside/o
utside number (conformation-dependent values) and (2) the side-chain length
(depends only on the residue type and does not depend on the side chain co
nformation). The results showed that the interface side chains tend to be b
ent away from the interacting helix. The most important finding, however, i
s that the side chains in the interface areas, on average, are shorter than
in the noninterface areas. Proteins 2000;40:429-435, (C) 2000 Wiley-Liss,
Inc.