Structural implications of SARS-CoV-2 Surface Glycoprotein N501Y mutation within receptor-binding domain [499-505] – computational analysis of the most frequent Asn501 polar uncharged amino acid mutations

Structural implications of SARS-CoV-2 Surface Glycoprotein N501Y mutation within receptor-binding domain [499-505] – computational analysis of the most frequent Asn501 polar uncharged amino acid mutations

The aim of this study was to evaluate the impact of the most frequent Asn501 polar uncharged amino acid mutations upon important structural properties of SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) Surface Glycoprotein RBD – hACE2 (human angiotensin-converting enzyme 2) heterodimer....

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Bibliographic Details
Main Author: Done Stojanov
Format: Article
Language:English
Published: Taylor & Francis Group 2023-03-01
Series:Biotechnology & Biotechnological Equipment
Subjects:
SARS-CoV-2
N501Y
mutation
COVID-19
surface glycoprotein
hydrogen bonds
Online Access:https://www.tandfonline.com/doi/10.1080/13102818.2023.2206492
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https://www.tandfonline.com/doi/10.1080/13102818.2023.2206492

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