SEGMENTATION OF SES FOR PROTEIN STRUCTURE
ANALYSIS
Virginio Cantoni, Riccardo Gatti, Luca Lombardi
Keywords: Protein structure analysis, protein-protein interaction, surface labeling, convex hull, distance transform
Abstract: The morphological complementarities of molecular surfaces provides insights for the identification and
evaluation of binding sites. A quantitative characterization of these sites is an initial step towards protein
based drug design. The final goal of the activity here presented is to provide a method that allows the
identification of sites of possible protein-protein and protein-ligand interaction on the basis of the
geometrical and topological structure of protein surfaces. The goal is to discover complementary regions
(that is with concave and convex segments that match each others) among different molecules. In particular,
we are considering the first step of this process: the segmentation of the protein surface in protuberances and
cavities through an approach based on an analysis of the molecule Convex Hull and on the Distance
Transform.