An In-Silico Technique: Prediction of Unknown Protein Structure from Sequences by Homology

Abstract

The structural characterization of protein sequences is one of the most common problems in biology. This task is usually facilitated by the accurate Three-Dimensional (3-D) structure of the protein. This paper was carried out to investigate and compare the most suitable software online tools for homology modeling of protein structure by obtaining few samples of proteins. Different length, known and unknown (3-D) proteins structures of bacteria, and viruses were obtained from Uniprot which do not have a Protein Data Bank Identifier (PDB ID). This paper used several tools, such CPHmodels-3.2, Phyre2, Swiss- Model, (PS)2-v2, and Robetta, for predicting, comparison and model generation, where CPHmodels-3.2 and Phyre2 Server, gave relatively better values. Proteins (3-D) structure was evaluated using PROSESS Server and the better evaluation to proteins structure was for the Phyre2 software online tool.