Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure, dynamics and free energy studies on the effect of point mutations on SARS-CoV-2 spike protein binding with ACE2 receptor.

PloS one - 1 Jan 2023

Rucker George, Qin Hong, Zhang Liqun

Abstract excerpt

The ongoing COVID-19 pandemic continues to infect people worldwide, and the virus continues to evolve in significant ways which can pose challenges to the efficiency of available vaccines and therapeutic drugs and cause future pandemic. Therefore, it is important to investigate the binding and interaction of ACE2 with different RBD variants. A comparative study using all-atom MD simulations was conducted on ACE2...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Angiotensin-Converting Enzyme 2
Share to COVID-19
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Pandemics

Share to Point Mutation

Share to Protein Binding

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 37796794
DOI: 10.1371/journal.pone.0289432
PMCID: PMC10553274

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure, dynamics and free energy studies on the effect of point mutations on SARS-CoV-2 spike protein binding with ACE2 receptor.PMID 37796794Read ↗

In silico binding profile characterization of SARS-CoV-2 spike protein and its mutants bound to human ACE2 receptor.Semantic proximity Read ↗

Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2.Semantic proximity Read ↗

In silico analysis of SARS-CoV-2 spike protein N501Y and N501T mutation effects on human ACE2 binding.Semantic proximity Read ↗

Mechanistic insights into the effects of key mutations on SARS-CoV-2 RBD-ACE2 binding.Semantic proximity Read ↗

Mechanistic Insights into the Effects of Key Mutations on SARS-CoV-2 RBD-ACE2 BindingSemantic proximity Read ↗

The role of S477N mutation in the molecular behavior of SARS-CoV-2 spike protein: An in-silico perspective.Semantic proximity Read ↗

Key residues of the receptor binding domain in the spike protein of SARS-CoV-2 mediating the interactions with ACE2: a molecular dynamics studySemantic proximity Read ↗

Binding Interactions between RBD of Spike-Protein and Human ACE2 in Omicron variantSemantic proximity Read ↗

Evolutionary and structural analysis elucidates mutations on SARS-CoV2 spike protein with altered human ACE2 binding affinity.Semantic proximity Read ↗

Evolutionary and structural analysis elucidates mutations on SARS-CoV2 spike protein with altered human ACE2 binding affinity.Semantic proximity Read ↗

Comparative Study of the Mutations Observed in the SARS-CoV-2 RBD Variants of Concern and Their Impact on the Interaction with the ACE2 Protein.Semantic proximity Read ↗

Molecular dynamics study on the strengthening behavior of Delta and Omicron SARS-CoV-2 spike RBD improved receptor-binding affinitySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.