“Woah! It's like Spotify but for academic articles.”

Instant Access to Thousands of Journals for just $30/month

Binding free energy calculations of galectin-3–ligand interactions

Binding free energy calculations of galectin-3–ligand interactions Abstract Galectins show remarkable binding specificity towards β-galactosides. A recently developed method for calculating binding free energies between a protein and its substrates has been used to evaluate the binding specificity of galectin-3. Five disaccharides and a tetrasaccharide were used as the substrates. The calculated binding free energies agree quite well with the experimental data and the ranking of binding affinities is well reproduced. For all the six protein–ligand complexes it was observed that electrostatic interactions oppose binding whereas the non-polar contributions drive complex formation. The observed binding specificity of galectin-3 for galactosides rather than glucosides is discussed in light of our results. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Protein Engineering, Design and Selection Oxford University Press

Binding free energy calculations of galectin-3–ligand interactions

Abstract

Abstract Galectins show remarkable binding specificity towards β-galactosides. A recently developed method for calculating binding free energies between a protein and its substrates has been used to evaluate the binding specificity of galectin-3. Five disaccharides and a tetrasaccharide were used as the substrates. The calculated binding free energies agree quite well with the experimental data and the ranking of binding affinities is well reproduced. For all the six protein–ligand complexes it was observed that electrostatic interactions oppose binding whereas the non-polar contributions drive complex formation. The observed binding specificity of galectin-3 for galactosides rather than glucosides is discussed in light of our results.
Loading next page...
 
/lp/oxford-university-press/binding-free-energy-calculations-of-galectin-3-ligand-interactions-TFHvldGI1r

Sorry, we don't have permission to share this article on DeepDyve,
but here are related articles that you can start reading right now: