Protein surface roughness accounts for binding free energy of Plasmepsin II‐ligand complexes

The calculation of absolute binding affinities for protein‐inhibitor complexes remains as one of the main challenges in computational structure‐based ligand design. The present work explored the calculations of surface fractal dimension (as a measure of surface roughness) and the relationship with e...

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Veröffentlicht in:	Journal of molecular recognition 2018-01, Vol.31 (1), p.n/a
Hauptverfasser:	Valdés‐Tresanco, Mario E., Valdés‐Tresanco, Mario S., Valiente, Pedro A., Cocho, Germinal, Mansilla, Ricardo, Nieto‐Villar, J.M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Approximation Aspartic Acid Endopeptidases - chemistry Binding sites Catalytic Domain Chemical compounds Computer applications Computer simulation Coordination compounds Crystal structure drug design Entropy fractal dimension Fractals Free energy Ligands Malaria Mathematical analysis molecular descriptor Molecular dynamics Molecular Dynamics Simulation Pharmacology plasmepsin II Protein Binding protein surface roughness Protozoan Proteins - chemistry Regression models Surface Properties Surface roughness Thermodynamics Vector-borne diseases
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