In this course, you will develop a fundamental understanding and will become conversant in the applications of several critical spectroscopy techniques to Structural Biology. Mainly through X-ray diffraction of crystals (XRD), but also Nuclear Magnetic Resonance (NMR) and Electron Microscopy (EM), the atomic view of the biological world is continuously expanding. Although this solves many mysteries of molecular function, our understanding of structure and function often requires the use of other complementary techniques, especially those that rely on the interaction between electromagnetic radiation and biological molecules, i.e., spectroscopy. These spectroscopic methods provide essential insights that are not accessible by the main structural techniques (XRD, NMR or EM), in the structural analysis of biomolecules, their dynamics, protein-protein or protein-ligand interactions, or the role of these biomolecules in a cellular environment. Overall, the aim is that you can use the acquired understanding of these techniques and apply it to a series of problems with examples from the literature, understanding at the same time their limitations, for their integration in your future projects. Current practice of Structural Biology is critically dependent on such integration. From a professional perspective, each of these techniques is a world in itself, and familiarity with its applications will also be useful in your future potential links with industry.
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