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

Stojanov, Done (2023) 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. Biotechnology & Biotechnological Equipment, 37 (1). p. 2206492. ISSN 1314-3530

Text Structural implications of SARS CoV 2 Surface Glycoprotein N501Y mutation within receptor binding domain 499 505 computational analysis of the most (1).pdf Download (3MB)

Abstract

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. Mutations N501Y, N501T and N501S were considered and their impact upon complex solubility, secondary motifs formation and intermolecular hydrogen bonding interface was analyzed. Results and findings are reported based on 50 ns run in Gromacs molecular dynamics simulation software. Special attention is paid on the biomechanical shifts in the receptor-binding domain (RBD) [499-505]: ProThrAsn(Tyr)GlyValGlyTyr, having substituted Asparagine to Tyrosine at position 501.

Item Type:	Article
Impact Factor Value:	2.116
Subjects:	Natural sciences > Biological sciences Natural sciences > Chemical sciences Natural sciences > Computer and information sciences
Divisions:	Faculty of Computer Science
Depositing User:	Done Stojanov
Date Deposited:	23 May 2023 11:45
Last Modified:	23 May 2023 11:45
URI:	https://eprints.ugd.edu.mk/id/eprint/31779

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