Computational Investigation of Hydrophobic Profile of Proteins in Coronaviruses

Abstract

The hydrophobic force is one of the most dominant factors in protein folding. A protein newlinebecomes functional only when it achieves its three-dimensional structure and stability newlineupon folding. For a better understanding of the hydrophobic effects and their function in newlineprotein folding, quantitative measurement of the hydrophobicity of amino acid side newlinechains is crucial. Hydrophobicity scales have been developed to classify the relative newlinehydrophobicity of different amino acids. These scales help researchers assess the newlinehydrophobic character of specific amino acids and predict their contributions to protein newlinefolding and stability. For the entire investigation researchers considered the spike newlineprotein of coronaviruses which is the main structural protein and also a multifunctional newlineprotein in SARS-CoV-2, SARS-CoV, and MERS-CoV. Computational tools/ newlinetechniques have been utilized to investigate the protein sequences of the three primary newlinespike proteins of SARS-CoV-2, SARS-CoV, and MERS-CoV. newlineThe researchers aim to investigate the hydrophobic distribution and its relative strength, newlinesecondary structure of spike protein sequences of three primary coronaviruses newlinecorresponding to the stretches of consecutive hydrophobic amino acid residues, and the newlineinterrelation between each aromatic and aliphatic hydrophobic residues by developing newlineand implementing computer programs. Besides the primary sequences, similar newlineinvestigations were carried out for other aligned sequences from different coronaviruses newlineand source organisms. newlineThis study explores how protein sequences in SARS-CoV-2, SARS-CoV and MERS- newlineCoV spike proteins encode hydrophobic interactions. Investigations provided an newlineestimate of hydrophobic distribution and its relative strength, indicating a hydrophobic newlinepattern. By examining the secondary structure in relation to the stretches of consecutive newlinehydrophobic amino acid residues, a better understanding of the folding patterns and newlinestability of the spike proteins might be gained.