Elegant Spin Labeling for Magnetic Resonance Experiments
It’s probably the most elegant solution for site-directed spin labeling ever: During the natural biosynthesis of a protein, magnetic markers are added directly to the cell in form of modified amino acids. The structure of the protein can now be ascertained by obtaining distance constraints in the nanometer range, by means of electron spin resonance spectroscopy – and can be done so inside the living cell, making it possible to examine protein folding in vivo.
The development of intercellular electron spin resonance spectroscopy is a good example of the research work done by Malte Drescher’s team. It develops and applies special spectroscopic methods for investigating the structure and dynamics of macromolecules in complex environments. “The overall aim is to elucidate the structure and dynamics of macromolecules right where they are at work, inside the cell or the nanoparticle, for example,” explains Prof. Dr. Malte Drescher, who holds the Heisenberg-professorship “Spectroscopy of Complex Systems”. Long-term, the young team plans to link imaging and spectroscopic methods in vivo.