Biological NMR (Nuclear Magnetic Resonance)
Leader: Ewen Lescop
This course unit in biological NMR aims to provide the minimum theoretical foundations of NMR to understand the NMR phenomenon and its applications at the interface between biology and chemistry. We will cover general concepts and specific methods useful for characterizing the structure and dynamics of biological macromolecules (proteins, etc.) and their interactions with other partners. The strengths of NMR will be highlighted (dynamic aspects of proteins, studies of primarily disordered proteins, studies within the cell, and molecular interactions). The course outline is as follows:
- Introduction to the NMR phenomenon
- 1D and 2D spectra
- NMR interactions (scalar and dipolar couplings)
- Some basics of calculating NMR pulse sequences
- Study of protein spectra of varying weights and flexibilities (tutorials)
- NMR signal assignment methods: theory and examples (tutorials, practicals)
- 3D structure calculation methods
- The relationship between spin relaxation and molecular motion
- Solid-state NMR
- Protein-ligand interactions: relationship between interaction equilibria/kinetics and NMR spectra. Examples of studies.
- NMR applied to truly disordered proteins or in-cell conditions
- Physical foundations of MRI imaging and principles of contrast agents in MRI.
The exam consists of a paper presentation followed by a discussion.
- Teaching coordinator: Mechulam Yves