SARS-CoV-2 omicron RBD forms a weaker binding affinity to hACE2 compared to Delta RBD in <i>in-silico</i> studies-Reference-Cited by-同舟云学术

SARS-CoV-2 omicron RBD forms a weaker binding affinity to hACE2 compared to Delta RBD in in-silico studies

Published:2023-06-22 Issue: Volume: Page:1-10
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Le Hoa Thanh¹²^ORCID,Tran Linh Hoang³⁴,Phung Huong Thi Thu⁵^ORCID

Affiliation:

1. Laboratory of Theoretical and Computational Biophysics, Advanced Institute of Materials Science, Ton Duc Thang University, Ho Chi Minh City, Vietnam

2. Faculty of Applied Sciences, Ton Duc Thang University, Ho Chi Minh City, Vietnam

3. Faculty of Civil Engineering, Ho Chi Minh City University of Technology (HCMUT), Ho Chi Minh City, Vietnam

4. Vietnam National University Ho Chi Minh City, Ho Chi Minh City, Vietnam

5. NTT Hi-Tech Institute, Nguyen Tat Thanh University, Ho Chi Minh City, Vietnam

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2023.2222827

Reference64 articles.

1. In silico study of SARS‐CoV‐2 spike protein RBD and human ACE‐2 affinity dynamics across variants and Omicron subvariants

2. GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers

3. Covid-19 Vaccine Effectiveness against the Omicron (B.1.1.529) Variant

4. The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling

5. In vitro data suggest that Indian delta variant B.1.617 of SARS‐CoV‐2 escapes neutralization by both receptor affinity and immune evasion