Highlights
Nuclear Magnetic Resonance is a unique and extremely powerful biophysical technique that provides detailed information about individual atoms in biological be used to solve a variety of biological and biomedical problems, including characterization of:
- Structure and dynamics for macromolecules (proteins and nucleic acids) including different functional states and short-living intermediates in vitro and in vivo (inside the living cells)
- Functional conformational changes and flexibility of macromolecules
- Allosteric pathways and mechanisms of signal transduction through protein structure
- Intrinsically disordered proteins (IDP)
- Molecular mechanisms of protein folding, misfolding and aggregations
- Ligand and drug binding including characterisation of binding sites and molecular contacts as well as thermodynamics and chemical kinetics of binding
- Protein-protein and protein-nucleotide interactions including transient multicomponent interactions .
This project is primarily designed to introduce you to this state-of-the-art technique and illustrate some practical aspects of modern protein NMR spectroscopy. Each section provides a brief introduction to the topic and several examples. You will need to answer 4 questions. This assessment forms 20% of the overall module mark.
Task 1: 2D NMR
Task 2: 3D NMR
Task 3: NMR peak assignments
Task 4: Ligand binding
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