A Topological Data Analysis of the Protein Structure

Abstract

Persistent homology is a tool from a set of methods called Topological data analysis, showing until nowadays a lot of success when it comes to application in biology since this latest uses metrics only for measuring similarities, Embedding the geometric details and focusing on the global shape is the key point making the success of persistent homology, this will be investigated in the paper since enormous work already done in the field and results seems to be endless, as an efficient topological data analysis tool. In this work we will be confirming the latest assumption (topology embeds geometry) by displaying the structure of COILED SERINE which is a protein estimated to constitute 3-5 percent of the encoded residues in most genomes, and giving a substitute of the optimal characteristic distance that can be used in the flexibility-rigidity index, a classic method used to simulate molecule movements and flexible behavior, when it comes to atomic rigidity functions. We will also analyze interesting patterns in the binding site of the beta sheet generated from the pdb file 2JOX. We will be detecting and giving a simple description of different patterns generated by using javaplex generating barcodes and linear statistical results as a summary statistics.