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

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

Journal of chemical information and modeling - 28 Dec 2020

Zou Junjie, Yin Jian, Fang Lei, Yang Mingjun, Wang Tianyuan, Wu Weikun, Bellucci Michael A, Zhang Peiyu

Abstract excerpt

The ability of coronaviruses to infect humans is invariably associated with their binding strengths to human receptor proteins. Both SARS-CoV-2, initially named 2019-nCoV, and SARS-CoV were reported to utilize angiotensin-converting enzyme 2 (ACE2) as an entry receptor in human cells. To better understand the interplay between SARS-CoV-2 and ACE2, we performed computational alanine scanning mutagenesis on the...

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

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutagenesis

Share to Protein Conformation

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Share to Thermodynamics

Source

Identifiers

PMID: 32786709
DOI: 10.1021/acs.jcim.0c00679

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Computational Prediction of Mutational Effects on SARS-CoV-2 Binding by Relative Free Energy Calculations.PMID 32786709Read ↗

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

E484K mutation in SARS-CoV-2 RBD enhances binding affinity with hACE2 but reduces interactions with neutralizing antibodies and nanobodies: Binding free energy calculation studies.Semantic proximity Read ↗

E484K mutation in SARS-CoV-2 RBD enhances binding affinity with hACE2 but reduces interactions with neutralizing antibodies and nanobodies: Binding free energy calculation studiesSemantic proximity Read ↗

Computational optimization of the SARS-CoV-2 receptor-binding-motif affinity for human ACE2Semantic proximity Read ↗

Accurate Evaluation on the Interactions of SARS-CoV-2 with Its Receptor ACE2 and Antibodies CR3022/CB6*Semantic proximity Read ↗

Computational prediction of the effect of mutations in the receptor-binding domain on the interaction between SARS-CoV-2 and human ACE2.Semantic proximity Read ↗

Quantitative analysis of ACE2 binding to coronavirus spike proteins: SARS-CoV-2 vs. SARS-CoV and RaTG13.Semantic proximity Read ↗

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

Interactions of the Receptor Binding Domain of SARS-CoV-2 Variants with hACE2: Insights from Molecular Docking Analysis and Molecular Dynamic SimulationSemantic proximity Read ↗

Differences between Omicron SARS-CoV-2 RBD and other variants in their ability to interact with cell receptors and monoclonal antibodies.Semantic proximity Read ↗

Computational Hot-Spot Analysis of the SARS-CoV-2 Receptor Binding Domain/ACE2 Complex*.Semantic proximity Read ↗

Probing the binding nature and stability of highly transmissible mutated variant alpha to omicron of SARS-CoV-2 RBD with ACE2 via molecular dynamics simulation.Semantic proximity Read ↗

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