The prediction of protein–ligand binding affinities using free energy perturbation (FEP) is becoming increasingly routine in structure-based drug discovery. Most FEP packages use molecular dynamics (M
The table shows the detailed contribution of energy components calculated using Poisson Boltzmann Surface Area (MM-PBSA) method for EhSAT1, EhSAT3 and their mutants to evaluate their binding activity.
The theory of receptor–ligand binding equilibria has long been well-established in biochemistry, and was primarily constructed to describe dilute aqueous solutions. Accordingly, few computational appr
The accurate prediction of the binding affinity changes of drugs caused by protein mutations is a major goal in clinical personalized medicine. We have developed an ensemble-based free energy approach