Scientific Program
Thursday May 5th 2016
Invitation: Zdeněk Hostomský, IOCB AS CR director
Opening: Jiří Vondrášek IOCB AS CR
Session 1 (18:00 - 19:30)
Chairman : Mikael Oliveberg
1.1 18:00 - 18:45 Janet Thornton (EMBL-EBI, United Kingdom)
The Evolution of enzyme function - a model for design
1.2 18:45 - 19:30 Alexander Wlodawer (National Cancer Institute, USA)
Design of proteins targeting HIV – I
19:30 - 21:00 Welcome drink, reception
Friday May 6th 2016
Session 2 (9:00 - 12:30)
Chairman : Nikolay Dokholyan
2.1 9:00 - 9:45 Dek Woolfson (University of Bristol, United Kingdom)
Exploring new protein folds and functions through de novo design
2.2 9:45 – 10:30 Scott Boyken (University of Washington in Seattle, USA)
Programmable protein interaction specificity
10:30 - 11:00 Coffee Break
2.3 11:00 - 11:45 Birte Höcker (Max Planck Institute, Germany)
Protein Design from subdomain sized fragments
2.4 11:45 - 12:30 Pietro Sormanni (Univeristy of Cambridge, United Kingdom)
A modular design strategy for the rational design of protein interactions
12:30 - 14:00 Lunch
Session 3 (14:00 - 18:30)
Chairman : Alex Wlodawer
3.1 14:00 - 14:45 Thomas Schiex (Institute for Agricultural Research, France)
Guaranteed energetic optimization, exploration and counting of sequence-conformation in Computational Protein Design
3.2 14:45-15:30 Jiří Damborský (ICRC Brno, Czech Republic)
Design and evolution of protein tunnels
3.3 15:30-16:15 Evžen Bouřa (IOCB AS CR, Czech Republic)
Protein design for macromolecular crystallography
16:15 - 16:45 Coffee Break
3.4 16:45 - 17:30 Mikael Oliveberg (Stockholm University, Sweden)
Protein stability in live cells
3.5 17:30 - 18:15 Simon Ebbinghaus (Ruhr-Universitat, Bochum, Germany)
Proteins in vivo - what determines the folding stability in the cell
18:15 - 19:00 Dinner buffet
19:00 - 19:30 Piotr Wardega (NanoTemper)
Advanced quantitative biomolecular analytics in free solution
19:00 - 22:00 Poster Session
Saturday 7th 2016
Session 4 (9:00 - 12:30)
Chairman : Barry Honig
4.1 9:00 - 9:45 David Eisenberg (University of California Los Angeles, USA)
Designed inhibitors of amyloid fibrils
4.2 9:45 - 10:30 Ingemar André (CPMS Lund, Sweden)
Computational design of protein and peptide self-assembly
10:30 - 11:00 Coffee Break
4.3 11:00 - 11:45 Barry Honig (Columbia University, USA)
How adhesion proteins are designed: The molecular basis of specific cell-cell recognition
4.4 11:45 - 12:30 Andrew Lovering (University of Birmingham, United Kingdom)
Unusual Proteins from the Bacterial Predator Bdellovibrio bacteriovorus
12:30 - 14:00 Lunch
Session 5 (14:00 - 18:30)
Chairman : Don Hilvert
5.1 14:00 - 14:45 Charlotte M. Deane (University of Oxford, United Kingdom)
Improving In Silico Therapeutic Antibody Design
5.2 14:45 - 15:30 Sarel J. Fleishman (Weizmann Institute of Science, Israel)
Computational design of novel antibodies and enzymes from fragments of natural ones
5.3 15:30 - 16:15 Selected talk from PPS Participants
5.3.1 15:30 - 15:45
Ivan Colluzza (University of Vienna, Austria)
Transferable coarse-grained potential for de novo protein folding and design
5.3.2 15:45 - 16:00
Perczel András (Eötvös L. Univ / Lab. of Structural Chem & Biol., Hungary)
Hidden folding intermediate by NMR: structural insights of an F I U transition
5.3.3 16:00 - 16:15
Kvido Stříšovský (IOCB AS CR, Czech Republic)
Keeping membrane proteins in check – deciphering nature’s design of an intramembrane cleaving protease
16:15 - 16:45 Coffee Break
5.4 16:45 - 17:30 Jurgen Haas (Swiss Institute of Bioinformatics, Switzerland)
Keeping Bad Bugs at Bay – Computational Engineering of the Trans-membrane Glycosyl-transferase PglB
5.5 17:30 - 18:15 Donald Hilvert (ETH Zurich, Switzerland)
Nearer to nature: design and optimization of artificial enzymes
20:00 - 23:00 Conference Dinner at Strahov Monastery
Sunday 8th 2016
Session 6 (9:30 - 11:00)
Chairman : Sarel J. Fleishman
6.1 9:30 - 10:15 Nikolay Dokholyan (University of North Carolina, Chapel Hill, USA)
Uncovering mysteries of ALS etiology
6.2 10:15 - 11:00 Michele Vendruscolo (Cambridge University, United Kingdom)
Using rational molecular design to combat protein misfolding diseases