Bridging scales in the coevolution of interacting proteins
Event details
| Date | 16.05.2017 |
| Hour | 14:00 |
| Speaker | Prof . Martin Weigt, Institut de biologie Paris-Seine, université Pierre et Marie Curie |
| Location | |
| Category | Conferences - Seminars |
BIOLOGICAL & STATISTICAL PHYSICS SEMINAR
Understanding protein−protein interactions (PPI) is central to our understanding of almost all complex biological processes. Computational tools exploiting rapidly growing genomic databases to characterize PPI are therefore urgently needed. Such methods should address multiple scales of PPI: (i) Between two interacting proteins, which residues are in contact across the interfaces? (ii) Inside a genome, which specific proteins interact and which do not? (iii) On evolutionary time scales, which protein-protein interactions are actually conserved across thousands of species? Statistical inference methods like the Direct-Coupling Analysis (DCA), have recently triggered considerable progress in using sequence data to connect these different scales, thereby helping to assemble quaternary protein structures and to predict conserved interactions between proteins. Besides evident bioinformatic applications in structural and systems biology, these methods help to deepen our understanding of the patterns of co-evolution between interacting proteins in general.
Understanding protein−protein interactions (PPI) is central to our understanding of almost all complex biological processes. Computational tools exploiting rapidly growing genomic databases to characterize PPI are therefore urgently needed. Such methods should address multiple scales of PPI: (i) Between two interacting proteins, which residues are in contact across the interfaces? (ii) Inside a genome, which specific proteins interact and which do not? (iii) On evolutionary time scales, which protein-protein interactions are actually conserved across thousands of species? Statistical inference methods like the Direct-Coupling Analysis (DCA), have recently triggered considerable progress in using sequence data to connect these different scales, thereby helping to assemble quaternary protein structures and to predict conserved interactions between proteins. Besides evident bioinformatic applications in structural and systems biology, these methods help to deepen our understanding of the patterns of co-evolution between interacting proteins in general.
Practical information
- Informed public
- Free
Organizer
- Prof. Paolo De Los Rios, Laboratory of Statistical Biophysics, Institute of Physic and Institute of Bioengineering
Contact
- Céline Burkhard, Laboratory of Statistical Biophysics (LBS)