Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes.
Schiebel, Johannes
Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes. [electronic resource] - Nature communications 09 2018 - 3559 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
2041-1723
10.1038/s41467-018-05769-2 doi
Benzamidines--pharmacology
Computer Simulation
Crystallography
Crystallography, X-Ray
Hydrogen Bonding
Ligands
Neutron Diffraction
Protein Binding
Serine Proteinase Inhibitors--pharmacology
Thermodynamics
Trypsin--chemistry
Water
Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes. [electronic resource] - Nature communications 09 2018 - 3559 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
2041-1723
10.1038/s41467-018-05769-2 doi
Benzamidines--pharmacology
Computer Simulation
Crystallography
Crystallography, X-Ray
Hydrogen Bonding
Ligands
Neutron Diffraction
Protein Binding
Serine Proteinase Inhibitors--pharmacology
Thermodynamics
Trypsin--chemistry
Water