In a previous study [(1987) J. Mol. Biol. 194, 663-673], we isolated t
en insertion/deletion mutants (indels) of the maltose binding protein
for which the maltose binding constant was only a little or not at all
affected. In this paper, we have localized these mutations in the rec
ently solved three-dimensional structure. Contrary to the general expe
ctation, most of the insertion/deletion modifications occurred within
elements of secondary structure. An analysis of the inserted residues
for three indels found within alpha helices allowed an interpretation
regarding protein structure accommodation to such modifications.