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Optimized Hydrophobic Interactions and Hydrogen Bonding at the Target-Ligand Interface Leads the Pathways of Drug-Designing
BACKGROUND: Weak intermolecular interactions such as hydrogen bonding and hydrophobic interactions are key players in stabilizing energetically-favored ligands, in an open conformational environment of protein structures. However, it is still poorly understood how the binding parameters associated w...
Autores principales: | Patil, Rohan, Das, Suranjana, Stanley, Ashley, Yadav, Lumbani, Sudhakar, Akulapalli, Varma, Ashok K. |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2922327/ https://www.ncbi.nlm.nih.gov/pubmed/20808434 http://dx.doi.org/10.1371/journal.pone.0012029 |
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