The alpha-helix [Pauling, L., Corey, R.B., & Branson, H.R. (1951) Proc
. Natl. Acad. Sci. U.S.A. 37, 205-211] is a common motif in both prote
ins and peptides. Despite intense investigation, predictive understand
ing of helices is still lacking. A recent hypothesis [Presta, L. G., &
Rose, G. D. (1988) Science 240, 1632-1641] proposed that the structur
al specificity of helices resides, in part, in those residues that fla
nk helix termini. If so, then signals that arrest helix propagation-i.
e., helix stop signals-should be found among these flanking residues.
Evidence is presented for the existence of one such signal, a reciproc
al backbone-side-chain hydrogen-bonding interaction, dubbed the cappin
g box. In proteins, the capping box is found uniquely at helix N-termi
ni. In peptides, the capping box can function as a helix stop signal,
as shown in the work of Kallenbach and co-workers.