Subject: Biological sciences
Subject: Chemical sciences
Subject: Computer and information sciences
Year: 2023
Type: Article
Type: PeerReviewed
Title: 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
Author: Stojanov, Done
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.
Publisher: Taylor & Francis
Relation: https://eprints.ugd.edu.mk/31779/
Identifier: oai:eprints.ugd.edu.mk:31779
Identifier: https://eprints.ugd.edu.mk/31779/1/Structural%20implications%20of%20SARS%20CoV%202%20Surface%20Glycoprotein%20N501Y%20mutation%20within%20receptor%20binding%20domain%20499%20505%20computational%20analysis%20of%20the%20most%20%281%29.pdfIdentifier: 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
Identifier: https://doi.org/10.1080/13102818.2023.2206492
