Structural and Functional Elucidation of IF-3 Protein of Chloroflexus aurantiacus Involved in Protein Biosynthesis: An In-Silico Approach

Abstract

<p>Chloroflexus aurantiacus is a thermophilic bacterium that produces a multitude of proteins<br>within its genome. Bioinformatics strategies can facilitate comprehending this organism through<br>functional and structural interpretation assessments.This study aimed to allocate the structure and<br>function through an in-silico approach required for bacterial protein biosynthesis. This in-silico<br>viewpoint provides copious properties, including the physicochemical properties, subcellular location,<br>three-dimensional structure, protein-protein interactions, and functional elucidation of the protein<br>(WP_012256288.1). The STRING program is utilized for the explication of protein-protein<br>interactions. The in-silico investigation documented the protein's hydrophilic nature with<br>predominantly alpha (α) helices in its secondary structure.The tertiary-structure model of the protein<br>has been shown to exhibit reasonably high consistency based on various quality assessment<br>methods.The functional interpretation suggested that the protein can act as a translation initiation<br>factor, a protein required for translation and protein biosynthesis. Protein-protein interactions also<br>demonstrated high credence that the protein interconnected with 30S ribosomal subunit involved in<br>protein synthesis. This study is bioinformatically examined that the protein (WP_012256288.1) is<br>affiliated in protein biosynthesis as a translation initiation factor IF-3 of C. aurantiacus. <br><br></p>