Protein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3

@inproceedings{Diehl2010ProteinFA,
  title={Protein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3},
  author={Carl Diehl and Olof Engstr{\"o}m and Tamara Delaine and Maria H{\aa}kansson and Samuel Genheden and Kristofer Modig and Hakon Leffler and Ulf Ryde and Ulf J Nilsson and Mikael Akke},
  booktitle={Journal of the American Chemical Society},
  year={2010}
}
Rational drug design is predicated on knowledge of the three-dimensional structure of the protein-ligand complex and the thermodynamics of ligand binding. Despite the fundamental importance of both enthalpy and entropy in driving ligand binding, the role of conformational entropy is rarely addressed in drug design. In this work, we have probed the conformational entropy and its relative contribution to the free energy of ligand binding to the carbohydrate recognition domain of galectin-3. Using… CONTINUE READING
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