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Updated: Feb 26, 2026

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
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Cómo nada aumenta la afinidad: Ligando hidrófobo a la bolsa de termolisina virtualmente vacía

Stefan G Krimmer1, Jonathan Cramer1, Johannes Schiebel1

  • 1Department of Pharmaceutical Chemistry, University of Marburg , Marbacher Weg 6, 35032 Marburg, Germany.

Journal of the American Chemical Society
|July 12, 2017
PubMed
Resumen

La bolsa hidrofóbica S1' de termolisina está prácticamente libre de agua, como lo confirmó la cristalografía y la calorimetría. El diseño del ligando demostró que este estado de hidratación de la bolsa tiene un impacto significativo en la afinidad de unión.

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