Statistical and computational physics of biomolecular systems
Anomalous relaxation and diffusion processes in biomolecular systems
The internal dynamics of biomolecular systems such as proteins is characterized by a vast spectrum of time scales and most of the dynamical modes are strongly overdamped and diffusive. Their time evolution and corresponding time correlation functions can be modeled by fractional Fokker-Planck equations, which generalize the idea of Markovian, i.e. memoryless small-step diffusion processes to stochastic processes with long-time memory. The keyword “anomalous relaxation” refers here to the strongly non-exponential decay of the corresponding time correlation functions. We have successfully applied and continue to apply such concepts to model quasielastic neutron scattering spectra and NMR relaxation spectra from proteins.
Minimal models for protein structure and dynamics
Elastic Network Models for proteins
An Elastic Network Model (ENM) describes a protein as a structured elastic object at a coarse-grained level. The most widely used ENMs represent a protein by its Cα atoms connected by springs. We have been developing, evaluating, and applying ENMs for many years, with applications including in particular the interpretation of low-resolution protein structures and the analysis of conformational transitions.