In silico equilibrium protein folding experiments
Research area: Computational Structural Biology
Associate members: Andrea Cavalli
Status: In progress
The process of how proteins reach their native basin of structures is poorly understood and constitutes an important problem in molecular biology. This process is called the protein folding problem, and is generally thought to proceed through large, concerted changes in structure.
In this project, we are studying the folding of two small proteins: the WW domain of Pin1 and Porcine peptide YY. These studies are carried out using molecular simulation combined with exact nuclear Overhauser enhancement data and/or chemical shift data obtained at multiple temperatures measured in the groups of collaborators Prof. Riek at the ETH in Zürich or Prof. Zerbe University of Zürich. Specifically, we are integrating all the experimental data with one simulation to obtain a full, thermodynamic and structural description of the protein folding process.