ABSTRACT
Understanding the interaction patterns among biological entities in a pathway can potentially reveal the role of the entities in biological systems. Although considerable effort has been contributed to this direction, querying biological pathways remained relatively unexplored. Querying is principally different in which we retrieve pathways satisfying a given property in terms of its topology, or constituents. One such property is subnetwork matching using various constituent parameters. In this paper, we introduce a logic based framework for querying biological pathways using a novel and generic subgraph isomorphism computation technique. We develop a graphical interface called IsoKEGG to facilitate flexible querying of KEGG pathways based on isomorphic pathway topologies as well as matching any combination of node names, types, and edges. It allows editing KGML represented query pathways and returns all isomorphic patterns in KEGG pathways satisfying a given query condition for further analysis.
Subject(s)
Data Mining/methods , Databases, Protein , Protein Interaction Mapping/methods , Signal Transduction/physiology , Software , User-Computer Interface , Algorithms , Computer Simulation , Database Management Systems , Logistic Models , Models, BiologicalABSTRACT
Improving the stability of proteins is an important goal in many biomedical and industrial applications. A logical approach is to emulate stabilizing molecular interactions found in nature. Disulfide bonds are covalent interactions that provide substantial stability to many proteins and conform to well-defined geometric conformations, thus making them appealing candidates in protein engineering efforts. Disulfide engineering is the directed design of novel disulfide bonds into target proteins. This important biotechnological tool has achieved considerable success in a wide range of applications, yet the rules that govern the stabilizing effects of disulfide bonds are not fully characterized. Contrary to expectations, many designed disulfide bonds have resulted in decreased stability of the modified protein. We review progress in disulfide engineering, with an emphasis on the issue of stability and computational methods that facilitate engineering efforts.
