Interactions among residues together with their interactions with the surro
unding medium determine the unique structure of globular proteins. An algor
ithm was recently developed to locate residues participating in cooperative
long-range interactions, called stabilization center residues, that are pr
imarily responsible for preventing the decay of the 3D structure. While our
statistical analysis showed that interactions of stabilization center resi
dues hardly influence the formation of the various secondary structure elem
ents, the distribution of the stabilization center residues is rather uneve
n among the secondary structure elements. Here we analyzed the frequency an
d distribution of the stabilization center residues and their interacting p
airs in secondary structure classes to learn about the effect of secondary
structure on the formation and properties of stabilization centers and abou
t the types of interactions responsible for stabilization of proteins of va
rious secondary structure classes. It was found that residues from the same
secondary structure tend to interact with each other in the stabilization
centers of all classes. It is also suggested that the folding-unfolding equ
ilibrium is governed by different principles for class all-a than for the r
est of the classes.