Disruption of Protein-Protein Interfaces
In Search of New Inhibitors
Nonfiction, Science & Nature, Science, Chemistry, Organic
| Author: | ISBN: | 9783642379994 | |
| Publisher: | Springer Berlin Heidelberg | Publication: | June 28, 2013 |
| Imprint: | Springer | Language: | English |
| Author: | |
| ISBN: | 9783642379994 |
| Publisher: | Springer Berlin Heidelberg |
| Publication: | June 28, 2013 |
| Imprint: | Springer |
| Language: | English |
"Disruption of Protein-Protein Interfaces" reviews the latest developments and future perspectives in drug discovery at protein-protein interfaces. The authors detail experimental and computational tools to tackle the subject and highlight the contribution of the Italian research community to the field. Evidence shows that blocking or modulating protein-protein interactions might lead to the development of useful new drugs. Consequently, in recent years great effort has been dedicated to unveiling the molecular details of protein-protein interfaces by structural techniques e.g. X-ray diffraction, NMR spectroscopy. This book, written and edited by leaders in the field, provides examples from the literature of successes and failures to develop drug-like molecules effective in interacting at protein-protein interfaces.
"Disruption of Protein-Protein Interfaces" reviews the latest developments and future perspectives in drug discovery at protein-protein interfaces. The authors detail experimental and computational tools to tackle the subject and highlight the contribution of the Italian research community to the field. Evidence shows that blocking or modulating protein-protein interactions might lead to the development of useful new drugs. Consequently, in recent years great effort has been dedicated to unveiling the molecular details of protein-protein interfaces by structural techniques e.g. X-ray diffraction, NMR spectroscopy. This book, written and edited by leaders in the field, provides examples from the literature of successes and failures to develop drug-like molecules effective in interacting at protein-protein interfaces.
