LIFE SCIENCES

Life Sciences

Principal Investigator: Bert de Groot , Computational Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, Göttingen

HPC Platform used: SuperMUC of LRZ

Local Project ID: pr85yi

Using Petascale system SuperMUC of the Leibniz Supercomputing Centre in Garching/Munich, scientists conducted simulations of mutated proteins to quantify and understand the mechanism of the change in population of binding compatible versus non-compatible states. This resulted in a predicted change in binding affinity which is a property that can be validated experimentally.

Life Sciences

Principal Investigator: Helmut Grubmüller , Theoretical and Computational Biophysics, Max-Planck-Institut für biophysikalische Chemie, Göttingen (Germany)

HPC Platform used: SuperMUC of LRZ

Local Project ID: FG-nups

The structural characterization of disordered proteins is an inherently under-determined problem: a small number of restraints are insufficient to uniquely define the conformations of a system with thousands of degrees of freedom. Molecular simulations, with their empirical force fields, can offer the additional information required to obtain conformational ensembles for disordered states of proteins. However, these simulations must contend with a massive sampling problem, which was successfully achieved by a team of scientists of the Max Planck Institute for Biophysical Chemistry in Göttingen using HPC system SuperMUC.