D. Y. Oztas

Atomistic Simulations and Deep Mutational Scanning of Protein Stability and Binding Interactions in the SARS-CoV-2 Spike Protein Complexes with Nanobodies: Molecular Determinants of Mutational Escape Mechanisms

Landscape-Based Mutational Sensitivity Cartography and Network Community Analysis of the SARS-CoV-2 Spike Protein Structures: Quantifying Functional Effects of the Circulating Variants

This study analyzes the functional effects of the D614G mutation in SARS-CoV-2 spike proteins using computational methods, revealing its role in enhancing infectivity through stability changes in residue interaction networks.

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

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.

Comparative Perturbation-Based Modeling of the SARS-CoV-2 Spike Protein Binding with Host Receptor and Neutralizing Antibodies : Structurally Adaptable Allosteric Communication Hotspots Define Spike Sites Targeted by Global Circulating Mutations

This study identifies structurally adaptable allosteric hotspots in the SARS-CoV-2 spike protein that are targeted by mutations and antibodies, showing their role in modulating binding affinity and stability.