Recent Developments and Applications of the MMPBSA Method

By Changhao Wang, D'Artagnan Greene, Li Xiao, Ruxi Qi, Ray Luo. Frontiers in Molecular Biosciences, 2018

586 citations recorded by the source corpus.

The Molecular Mechanics Poisson-Boltzmann Surface Area (MMPBSA) approach has been widely applied as an efficient and reliable free energy simulation method to model molecular recognition, such as for protein-ligand binding interactions. In this review, we focus on recent developments and applications of the MMPBSA method. The methodology review covers solvation terms, the entropy term, extensions to membrane proteins and high-speed screening, and new automation toolkits. Recent applications in various important biomedical and chemical fields are also reviewed. We conclude with a few future directions aimed at making MMPBSA a more robust and efficient method.

Subfields: Computational Theory and Mathematics, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/2129086682caeef47a44be924a1a3903996e6a32

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Computational Theory and Mathematics

1. Giulio Rastelli
2. Luca Pinzi

In Molecular Biology

1. Giulio Rastelli
2. Luca Pinzi

Citations in the corpus

• Molecular Docking: Shifting Paradigms in Drug Discovery (2019, background): “However, although the latter approaches are more accurate than docking scoring functions, or even other free energy methods as MM-PBSA and MM-GBSA, in predicting ligand-protein affinity, they are computationally expensive, therefore potentially less suitable for the screening of large libraries of c”