| (*)Students understand fundamental properties of proteins using key concepts from physical chemistry such as stability, kinetics, energetics, molecular structure, dynamics, degrees of freedom, entropy (k2). They understand how chemical or physical perturbations (pressure, pH, denaturants, isotope exchange) can be used to study key aspects of protein folding and stability using equilibrium and transient techniques (k4). Students know about the importance of intrinsically disordered proteins in biology and disease (k2). Students can devise protocols to study protein folding, aggregation, and interactions using advanced spectrometric and spectroscopic methods (k3,k6).
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(*)- Intrinsically disorder proteins
- Protein folding, structure and stability
- Advanced methods to study proteins, like NMR and MS
- H/D exchange
- High Pressure NMR
- Microscale thermophoresis and protein-ligand interactions
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