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Structural and functional aspects of osmolyte taurine are detailed, including its sulfonated amino acid structure and how it contributes to maintaining protein folding under stress conditions.

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![Figure 10: Structural and functional aspects of osmolyte taurine are detailed, including its sulfonated amino acid structure and how it contributes to maintaining protein folding under stress conditions.]()

> Source: Mujtaba Aamir Bhat et al. "Expedition into Taurine Biology: Structural Insights and Therapeutic Perspective." *Biomolecules*, 2020. PMID: [32516961](https://pubmed.ncbi.nlm.nih.gov/32516961/)
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  <img src="" alt="Structural and functional aspects of osmolyte taurine are detailed, including its sulfonated amino acid structure and how it contributes to maintaining protein folding under stress conditions." />
  <figcaption>Figure 10. Structural and functional aspects of osmolyte taurine are detailed, including its sulfonated amino acid structure and how it contributes to maintaining protein folding under stress conditions.<br>  Source: Mujtaba Aamir Bhat et al. "Expedition into Taurine Biology: Structural Insights and Therapeutic Perspective." <em>Biomolecules</em>, 2020. PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/32516961/">32516961</a></figcaption>
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