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.
Segmentation of SES for protein structure analysis
CANTONI, VIRGINIO;LOMBARDI, LUCA
2010-01-01
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
