Description
Radius of gyration and hydrogen bond dynamics from molecular dynamics simulations of the astaxanthin-protein complex are tracked, providing evidence for stable binding interactions associated with oxidative stress-mediated antibacterial activity.
Figure 3
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Astaxanthin-Mediated Bacterial Lethality: Evidence from Oxidative Stress Contribution and Molecular Dynamics Simulation.Cite This Figure
![Figure 3: Radius of gyration and hydrogen bond dynamics from molecular dynamics simulations of the astaxanthin-protein complex are tracked, providing evidence for stable binding interactions associated with oxidative stress-mediated antibacterial activity.]() > Source: Jamiu Olaseni Aribisala et al. "Astaxanthin-Mediated Bacterial Lethality: Evidence from Oxidative Stress Contrib." *Oxidative medicine and cellular longevity*, 2021. PMID: [34925700](https://pubmed.ncbi.nlm.nih.gov/34925700/)
<figure> <img src="" alt="Radius of gyration and hydrogen bond dynamics from molecular dynamics simulations of the astaxanthin-protein complex are tracked, providing evidence for stable binding interactions associated with oxidative stress-mediated antibacterial activity." /> <figcaption>Figure 3. Radius of gyration and hydrogen bond dynamics from molecular dynamics simulations of the astaxanthin-protein complex are tracked, providing evidence for stable binding interactions associated with oxidative stress-mediated antibacterial activity.<br> Source: Jamiu Olaseni Aribisala et al. "Astaxanthin-Mediated Bacterial Lethality: Evidence from Oxidative Stress Contrib." <em>Oxidative medicine and cellular longevity</em>, 2021. PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/34925700/">34925700</a></figcaption> </figure>