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We observed from amino acid usage patterns that spike proteins are associated with a diversity of mutational changes and most important underlying cause of variation of amino acid usage is the changes in hydrophobicity of spike proteins. The changing patterns of hydrophobicity of spike proteins over time and its influence on the receptor binding affinity provides crucial information on the SARS\u2010CoV\u20102 interaction with human receptor. Our results also show that spike proteins have evolved to prefer more hydrophobic residues over time. The present study provides a comprehensive analysis of molecular sequence data to consider that mutational variants might play a crucial role in modulating the virulence and spread of the virus and has immediate implications for therapeutic strategies.<\/jats:p>","DOI":"10.1002\/iub.2577","type":"journal-article","created":{"date-parts":[[2021,11,15]],"date-time":"2021-11-15T09:24:03Z","timestamp":1636968243000},"page":"213-220","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Underlying selection for the diversity of spike protein sequences of\n                    <scp>SARS\u2010CoV<\/scp>\n                    \u20102"],"prefix":"10.1002","volume":"74","author":[{"given":"Manisha","family":"Ghosh","sequence":"first","affiliation":[{"name":"Division of Bioinformatics ICMR\u2010National Institute of Cholera and Enteric Diseases  Kolkata 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