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...

Descripción completa

Detalles Bibliográficos
Autores principales: Patil, Rohan, Das, Suranjana, Stanley, Ashley, Yadav, Lumbani, Sudhakar, Akulapalli, Varma, Ashok K.
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2010
Materias:
Research Article
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

Internet

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

Ejemplares similares