Author

G. M. Verkhivker

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2

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Approach:deep learning· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Assay:structural biology· 2 Organism:virus· 2 Research Focus:cell-cell communication· 1 Assay:proteomics· 1 Approach:simulation· 1

Frequent Co-Authors

S. Agajanian· 2 shared D. Y. Oztas· 1 shared G. Gupta· 1 shared K. Krishnan· 1 shared R. Kassab· 1 shared

Activity by Year

2021-2022 · peak 1/yr

Co-Author Collaboration Network

5 top collaborators · 6 mutual co-author links

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2 shared papersBiophysics

S. Agajanian

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2 papers

Recent·Most cited

BiophysicsbioRxivPreprintApr 11, 2022

Hierarchical Computational Modeling and Dynamic Network Analysis of Allosteric Regulation in the SARS-CoV-2 Spike Omicron Trimer Structures: Omicron Mutations Cooperate to Allosterically Control Balance of Protein Stability and Conformational Adaptability

G. M. Verkhivker, S. Agajanian, R. Kassab, K. Krishnan

This study uses computational modeling to analyze how Omicron mutations in the SARS-CoV-2 spike protein regulate structural stability and conformational adaptability through allosteric networks.

DOI 10.1101/2022.04.11.487920

virusstructural biology

𝕏 PostBluesky

BiophysicsbioRxivApr 13, 2021

Dynamic Profiling of Binding and Allosteric Propensities of the SARS-CoV-2 Spike Protein with Different Classes of Antibodies: Mutational and Perturbation-Based Scanning Reveal Allosteric Duality of Functionally Adaptable Hotspots

G. M. Verkhivker, S. Agajanian, D. Y. Oztas, G. Gupta

This study uses atomistic simulations and mutational scanning to analyze how different antibodies affect the allosteric properties of SARS-CoV-2 spike protein residues, revealing how mutations at K417, E484, and N501 influence antibody resistance.

DOI 10.1021/acs.jctc.1c00372

virusstructural biology

𝕏 PostBluesky