Article ; Online: Unique amino acid substitution in RBD region of SARS-CoV-2 Omicron XAY.2
bioRxiv
Abstract: We attempted to explain the rare mutation at the receptor binding domain of the spike protein in the XAY.2 variant of SARS-CoV-2 from the perspective of hydrophobic interactions. We propose that decreasing hydrophobicity at position 446 and 486 of the ... ...
Abstract | We attempted to explain the rare mutation at the receptor binding domain of the spike protein in the XAY.2 variant of SARS-CoV-2 from the perspective of hydrophobic interactions. We propose that decreasing hydrophobicity at position 446 and 486 of the RBD region of the spike protein might affect the infectivity of SARS-CoV-2. We also estimated the probable mutations at the 446 and 486 position the virus may acquire, leading to a decreased hydrophobicity. |
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Keywords | covid19 |
Language | English |
Publishing date | 2023-01-09 |
Publisher | Cold Spring Harbor Laboratory |
Document type | Article ; Online |
DOI | 10.1101/2023.01.09.523246 |
Database | COVID19 |
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