The maximal and current accuracy of rigorous protein-ligand binding free energy calculations
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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1 Online-Ressource.
- Language
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Englisch
- Bibliographic citation
-
The maximal and current accuracy of rigorous protein-ligand binding free energy calculations ; volume:6 ; number:1 ; day:14 ; month:10 ; year:2023 ; pages:1-12 ; date:12.2023
Communications chemistry ; 6, Heft 1 (14.10.2023), 1-12, 12.2023
- Creator
-
Ross, Gregory A.
Lu, Chao
Scarabelli, Guido
Albanese, Steven K.
Houang, Evelyne
Abel, Robert
Harder, Edward D.
Wang, Lingle
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s42004-023-01019-9
- URN
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urn:nbn:de:101:1-2024020210170995930307
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:37 AM CEST
Data provider
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Ross, Gregory A.
- Lu, Chao
- Scarabelli, Guido
- Albanese, Steven K.
- Houang, Evelyne
- Abel, Robert
- Harder, Edward D.
- Wang, Lingle
- SpringerLink (Online service)
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Protein-ligand interactions
Free energy calculations of protein-ligand complexes with computational molecular dynamics
Functional dynamics of protein-ligand interactions
Automation of absolute protein-ligand binding free energy calculations for docking refinement and compound evaluation
DrugscoreMapsvisualizing similarities in protein-ligand interactions
A chemogenomics view on protein-ligand spaces
Mathematical modelling of multi-site protein-ligand interactions
The influence of protonation in protein-ligand docking
The influence of protonation in protein-ligand docking
Thermophoresis of electrolyte solutions and protein-ligand systems
Ensembling methods for protein-ligand binding affinity prediction
Water Networks Repopulate Protein–Ligand Interfaces with Temperature
Protein-ligand interactions
Free energy calculations of protein-ligand complexes with computational molecular dynamics
Functional dynamics of protein-ligand interactions
Automation of absolute protein-ligand binding free energy calculations for docking refinement and compound evaluation
DrugscoreMapsvisualizing similarities in protein-ligand interactions
A chemogenomics view on protein-ligand spaces
Mathematical modelling of multi-site protein-ligand interactions
The influence of protonation in protein-ligand docking
The influence of protonation in protein-ligand docking
Thermophoresis of electrolyte solutions and protein-ligand systems
Ensembling methods for protein-ligand binding affinity prediction