Crystallography sets the basis to understand the structural features of many biomolecules, from proteins to RNA and DNA. However, in vivo, protein-protein contacts, protein-lipid interactions, protein-DNA complex formation, conformational changes triggered by a plethora of stimuli, etc. modify the secondary/tertiary and quaternary structure of biomolecules, changing their function. Trapping each state of a functional cycle in a crystal is a tremendous challenge in the field, but the conformational changes of the biomolecules, and their interactions in living cells is of major interest in many areas of biological research. Spectroscopic techniques such as Förster (Fluorescence) Resonance Energy Transfer (FRET), Nuclear Magnetic Resonance (NMR), and Electron Paramagnetic Resonance (EPR) offer biophysical tools to investigate intra- and inter-molecular distances between amino acids or engineered probes in biomolecules under different conditions, from aqueous to membrane environments, in bulk or in single molecules, in vitro or in vivo conditions. Theoretical and experimental aspects of several biophysical approaches will be covered in the course. The students will present articles describing biophysical studies involving distance measurements in biomolecules, with special focus on the advantages/disadvantages of the technique chosen, and the relevance of the obtained information for the understanding of structural and functional aspects of the system under investigation. Schließen