Pages that link to "Q56975687"

The following pages link to Binding affinities in the SAMPL3 trypsin and host–guest blind tests estimated with the MM/PBSA and LIE methods (Q56975687):

Displaying 14 items.

• The MM/PBSA and MM/GBSA methods to estimate ligand-binding affinities (Q27012984) (← links)
• Effect of explicit water molecules on ligand-binding affinities calculated with the MM/GBSA approach. (Q30362956) (← links)
• Assessing the performance of MM/PBSA and MM/GBSA methods. 4. Accuracies of MM/PBSA and MM/GBSA methodologies evaluated by various simulation protocols using PDBbind data set. (Q30835329) (← links)
• Parameterization of an effective potential for protein-ligand binding from host-guest affinity data. (Q30986053) (← links)
• Large scale affinity calculations of cyclodextrin host-guest complexes: Understanding the role of reorganization in the molecular recognition process. (Q34065083) (← links)
• Binding-affinity predictions of HSP90 in the D3R Grand Challenge 2015 with docking, MM/GBSA, QM/MM, and free-energy simulations (Q37363075) (← links)
• Improvements, trends, and new ideas in molecular docking: 2012-2013 in review. (Q38390892) (← links)
• Machine Learning Accelerates MD-based Binding-Pose Prediction between Ligands and Proteins (Q42695969) (← links)
• Recent Developments and Applications of the MMPBSA Method (Q47713335) (← links)
• Binding affinities of the farnesoid X receptor in the D3R Grand Challenge 2 estimated by free-energy perturbation and docking. (Q48023567) (← links)
• Predicting hydration free energies with chemical accuracy: the SAMPL4 challenge (Q48887633) (← links)
• Comparison of end-point continuum-solvation methods for the calculation of protein-ligand binding free energies (Q57127575) (← links)
• MM/GBSA and LIE estimates of host-guest affinities: dependence on charges and solvation model (Q82599858) (← links)
• Free-energy perturbation and quantum mechanical study of SAMPL4 octa-acid host-guest binding energies (Q87611444) (← links)