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

RBD spatial orientation of the spike protein and its binding to ACE2: insight into the high infectivity of the SARS-CoV-2 Delta variant from MD simulations.

Physical chemistry chemical physics : PCCP - 12 Oct 2022

Lv Nan, Cao Zexing

Abstract excerpt

The spike glycoprotein on the surface of the SARS-CoV-2 envelope plays an important role in its invasion into host cells. The binding of the spike glycoprotein RBD to the angiotensin-converting enzyme 2 (ACE2) receptor as a critical step in the spread of the virus has been explored intensively since the outbreak of COVID-19, but the high transmissibility of the virus such as the Delta variant is still not fully...

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 Mutation

Share to Protein Binding

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Source

Identifiers

PMID: 36168828
DOI: 10.1039/d2cp03425e

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

RBD spatial orientation of the spike protein and its binding to ACE2: insight into the high infectivity of the SARS-CoV-2 Delta variant from MD simulations.PMID 36168828Read ↗

Featuring ACE2 binding SARS-CoV and SARS-CoV-2 through a conserved evolutionary pattern of amino acid residuesSemantic proximity Read ↗

Computational study of the strong binding mechanism of SARS-CoV-2 spike and ACE2Semantic proximity Read ↗

Structural perspective of the interactions of ACE2 and SARS CoV-2 Spike protein RBDSemantic proximity Read ↗

Differential Interactions between Human ACE2 and Spike RBD of SARS-CoV-2 Variants of ConcernSemantic proximity Read ↗

Structural basis for receptor-binding domain mobility of the spike in SARS-CoV-2 BA.2.86 and JN.1.Semantic proximity Read ↗

Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2Semantic proximity Read ↗

Surface charge changes in spike RBD mutations of SARS-CoV-2 and its variant strains alter the virus evasiveness via HSPGs: A review and mechanistic hypothesis.Semantic proximity Read ↗

Assessment of mutations on RBD in the Spike protein of SARS-CoV-2 Alpha, Delta and Omicron variants.Semantic proximity Read ↗

Binding Interactions between Receptor-Binding Domain of Spike Protein and Human Angiotensin Converting Enzyme-2 in Omicron Variant.Semantic proximity Read ↗

Sequence variation of SARS-CoV-2 spike protein may facilitate stronger interaction with ACE2 promoting high infectivitySemantic proximity Read ↗

Mechanistic origin of different binding affinities of SARS-CoV and SARS-CoV-2 spike RBDs to human ACE2Semantic 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 ↗

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