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

12 April 2021, Version 2
This content is a preprint and has not undergone peer review at the time of posting.


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


Chloroflexus aurantiacus
translation initiation factor IF-3
Homology modeling
Protein-protein interaction
, Functional annotation
Protein synthesis


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