Subject: The topic of the course deals with protein sequence analysis and protein structure prediction. The students have to conceive, design, develop, test and validate a computational program to predict the three-dimensional structure of a protein from its sequence of amino acids. The sequences of interest come from wet-lab experiments realized by M2 students enrolled in the Master "Biologie Santé" from Univ Paris-Sud - Univ Paris-Saclay.

Question: Given a protein primary sequence, what is the most probable / stable 3D fold adopted by the protein in solution?

Expected product: The project unfolds in two steps: ( i ) domain annotation based on profile-profile comparison and ( ii ) identification of the most stable 3D fold by threading. Each team is in charge of one of the two steps. Teams pair up halfway through the project to integrate the two steps into a final complete executable. The program has to be handled with a documentation.

Referent teachers: E. Laine for Sorbonne University, A. Lopes for UPSUD-UPSaclay.

Jury members: J. Andreani (I2BC, Saclay), M. Baaden (IBPC, Paris), C. Mayer (Institut Pasteur, Paris), J. Söding (Max Planck, Göttingen), P. Tuffery (U. de Paris, Paris)

Challenge-Colloquium day: It will take place on the 13th of January 2020, in Paris.