Molecular dynamics analysis of a flexible loop at the binding interface of the SARS‐CoV‐2 spike protein receptor‐binding domain

Since the identification of the SARS‐CoV‐2 virus as the causative agent of the current COVID‐19 pandemic, considerable effort has been spent characterizing the interaction between the Spike protein receptor‐binding domain (RBD) and the human angiotensin converting enzyme 2 (ACE2) receptor. This has...

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Bibliographic Details
Published in:	Proteins, structure, function, and bioinformatics Vol. 90; no. 5; pp. 1044 - 1053
Main Authors:	Williams, Jonathan K., Wang, Baifan, Sam, Andrew, Hoop, Cody L., Case, David A., Baum, Jean
Format:	Journal Article
Language:	English
Published:	Hoboken, USA John Wiley & Sons, Inc 01.05.2022 Wiley Subscription Services, Inc
Subjects:	ACE2 Angiotensin Angiotensin-Converting Enzyme 2 Binding Binding Sites coronavirus COVID-19 Crystal structure Flexibility Humans Molecular dynamics Molecular Dynamics Simulation Mutation Pandemics Peptidyl-dipeptidase A Protein Binding protein conformation protein dynamics protein modeling Protein structure Proteins Receptors SARS-CoV-2 Severe acute respiratory syndrome Severe acute respiratory syndrome coronavirus 2 Special issue: SARS‐CoV‐2 special issue for Proteins spike glycoprotein Spike Glycoprotein, Coronavirus - chemistry Spike protein Viral diseases SARS-CoV-2 spike glycoprotein molecular dynamics simulation protein dynamics coronavirus protein conformation protein modeling
ISSN:	0887-3585, 1097-0134, 1097-0134
Online Access:	Get full text
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