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Protein-Ligand Interaction Energies from Quantum-Chemical Fragmentation Methods: Upgrading the MFCC-Scheme with
Johannes R Vornweg1, Christoph R Jacob1
1Institute of Physical and Theoretical Chemistry, Technische Universität Braunschweig, Gaußstr. 17, Braunschweig 38106, Germany.
The Journal of Physical Chemistry. B
|November 17, 2024
Summary
We enhanced the molecular fractionation with conjugate caps (MFCC) method by incorporating many-body contributions. This significantly improves the accuracy of protein-ligand interaction energy calculations, achieving errors below 20 kJ/mol.
Area of Science:
- Computational chemistry
- Biophysics
- Molecular modeling
Background:
- Quantum-chemical fragmentation methods are crucial for calculating protein-ligand interactions.
- The standard molecular fractionation with conjugate caps (MFCC) scheme has limitations in accuracy.
Purpose of the Study:
- To improve the accuracy of the MFCC scheme for protein-ligand interaction energy calculations.
- To develop a more precise computational approach for molecular interactions.
Main Methods:
- Upgrading the MFCC scheme by incorporating many-body contributions.
- Extending the previously developed MFCC-MBE(2) scheme.
- Testing the enhanced scheme on a diverse set of protein-ligand complexes.
Main Results:
- The enhanced MFCC scheme with many-body contributions significantly reduces errors in protein-ligand interaction energies.
- Achieved general accuracy below 20 kJ/mol.
- Demonstrated systematic error reduction with higher-order many-body contributions.
Conclusions:
- The upgraded MFCC scheme provides highly accurate protein-ligand interaction energies.
- This method serves as an excellent foundation for developing accurate machine learning potentials for biomolecular systems.
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