Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
Trypsin is a serine protease. Here the authors present the high resolution X-ray and neutron diffraction structures of uncomplexed and inhibitor bound trypsin that provide insights into the geometry of H-bonds in the active site of the enzyme and molecular dynamics simulations reveal the kinetics of...
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Autores principales: | Johannes Schiebel, Roberto Gaspari, Tobias Wulsdorf, Khang Ngo, Christian Sohn, Tobias E. Schrader, Andrea Cavalli, Andreas Ostermann, Andreas Heine, Gerhard Klebe |
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Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
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Materias: | |
Acceso en línea: | https://doaj.org/article/dfa101099f7848ffada5601ea4aa65b1 |
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