In the preceding course "Biophysical Chemistry I" in SS2019 we introduced several biophysical techniques such as cryo-EM, X-ray, CD spectroscopy, FRET, FCS, super resolution microscopy, NMR and EPR which have a fundamental role in the characterization of proteins.

In this course, we will goo deeper into the magnetic resonance techniques, providing the fundamental physical background necessary to understand how this spectroscopy works. Magnetic Resonance Techniques such as NMR (nuclear magnetic resonance) and EPR (electron paramagnetic resonance) have a big impact in unveiling structural and functional properties of biomolecules and their principles rely on quantum mechanical rules.

If you like quantum mechanics, are interested in understanding how a magnetization vector is rotated by a radiofrequency pulse, which magnetic interactions provide an atomic resolution structure of a protein via NMR, or if you want to know how strong can be a dipolar coupling between two magnetic dipole moments of two electron radicals, and how we measure nanometer distances between spin labels in proteins via EPR... join the course.

The course will start from the very basic introduction of a magnetic dipole moment in classical mechanics, and will bring the students to the quantum mechanical description of spin Hamiltonians. Key biological applications of NMR and EPR will be given at the end of the course.

Exercises will be provided to facilitate the understanding of the topics introduced in the lectures.