Protein beta-sheets can be regarded as surfaces. Two surfaces can be c
onnected along a common edge to form a larger surface, or two edges of
a surface can coalesce to form a closed sheet such as a beta-barrel.
Singular points an locations where these connections are not perfect.
In protein beta-sheets, a singular point is characterized by a residue
separating two beta-ladders. In this paper, we study the singular poi
nts of protein beta-sheets from the surface topologic viewpoint. summa
rize our search results from the protein structural data in the Protei
n Data Bank. and present examples where singular points are near the a
ctive sites and may contribute to forming the proper relative position
s of catalytic residues.