Novel techniques for protein structure characterization using graph representation of proteins

Official URL: http://192.168.1.20/record=b1293732 (Table of Contents)

Proteins exhibit an infinite variety of structures. Around 50K 3D structures of proteins exist in PDB database among unlimited possibilities. The three dimensional structure of a protein is crucial to its function. Even within a common structure family, proteins vary in length, size, and sequence. This variation is the reflection of evolution on protein sequences. The intrinsic information in protein structures can be captured by their graph representations. The structural similarities between protein families can be deduced using their structural features such as connectivity, betweenness, and cliquishness. Most of the structure comparison and alignment methods use all atom coordinates that’s why they need reliable full atom representation of proteins which is difficult to obtain using experimental methods. These methods can be used for variety of problems in bioinformatics such as protein fold prediction, function annotation, domain prediction, and fold classification. Our approach can capture the same knowledge by using much less information from the actual structure. In this thesis, we used graph representations of proteins and graph theoretical properties to discriminate native and non-native proteins. Then we used these methods to find out overall and local similarity of protein structures by using dynamic programming. Afterward, local alignment using dynamic programming is used to determine the function of a protein. Moreover, sub graph matching algorithms was employed for domain prediction. In order to find the correct fold we also developed a genetic algorithm based threading approach. All these applications gave better or comparable results to state of the art.