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

Free Energy Perturbation Calculations of Mutation Effects on SARS-CoV-2 RBD::ACE2 Binding Affinity.

Journal of molecular biology - 1 Aug 2023

Sergeeva Alina P, Katsamba Phinikoula S, Liao Junzhuo, Sampson Jared M, Bahna Fabiana, Mannepalli Seetha, Morano Nicholas C, Shapiro Lawrence, Friesner Richard A, Honig Barry

Abstract excerpt

The strength of binding between human angiotensin converting enzyme 2 (ACE2) and the receptor binding domain (RBD) of viral spike protein plays a role in the transmissibility of the SARS-CoV-2 virus. In this study we focus on a subset of RBD mutations that have been frequently observed in infected individuals and probe binding affinity changes to ACE2 using surface plasmon resonance (SPR) measurements and free...

Read the complete abstract on PubMed

Topics

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

Share to Protein Domains
Share to Angiotensin-Converting Enzyme 2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Binding

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 37355034
DOI: 10.1016/j.jmb.2023.168187
PMCID: PMC10286572

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Free Energy Perturbation Calculations of Mutation Effects on SARS-CoV-2 RBD::ACE2 Binding Affinity.PMID 37355034Read ↗

Free energy perturbation calculations of mutation effects on SARS-CoV-2 RBD::ACE2 binding affinitySemantic proximity Read ↗

Single-Molecule Investigation of the Binding Interface Stability of SARS-CoV-2 Variants with ACE2Semantic proximity Read ↗

Impact of the temperature on the interactions between common variants of the SARS-CoV-2 receptor binding domain and the human ACE2.Semantic proximity Read ↗

Mutation N501Y in RBD of Spike Protein Strengthens the Interaction between COVID-19 and its Receptor ACE2Semantic proximity Read ↗

Computational Prediction of Mutational Effects on the SARS-CoV-2 Binding by Relative Free Energy CalculationsSemantic proximity Read ↗

Computational Prediction of Mutational Effects on SARS-CoV-2 Binding by Relative Free Energy Calculations.Semantic proximity Read ↗

Mutational Effect of Some Major COVID-19 Variants on Binding of the S Protein to ACE2.Semantic proximity Read ↗

N501Y and K417N Mutations in the Spike Protein of SARS-CoV-2 Alter the Interactions with Both hACE2 and Human-Derived Antibody: A Free Energy of Perturbation Retrospective Study.Semantic proximity Read ↗

Deciphering the free energy landscapes of SARS-CoV-2 wild type and Omicron variant interacting with human ACE2.Semantic proximity Read ↗

Impact of the Temperature on the Interactions Between Common Variants of the SARS-CoV-2 Receptor Binding Domain and the Human ACE2Semantic proximity Read ↗

The N501Y and K417N mutations in the spike protein of SARS-CoV-2 alter the interactions with both hACE2 and human derived antibody: A Free energy of perturbation studySemantic proximity Read ↗

Missense variants in human ACE2 strongly affect binding to SARS-CoV-2 Spike providing a mechanism for ACE2 mediated genetic risk in Covid-19: A case study in affinity predictions of interface variants.Semantic proximity Read ↗

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