Course Curriculum
- Biomolecular Structures: Molecule dimensions and the surrounding environment.
- Biomolecular Interactions: Protein-protein, protein-ligand and protein-DNA interactions.
- Molecular Recognition: Association and dissociation constants, binding energy, examples in molecular recognition, ion charges and stabilization. Entropic contributions in protein-protein complexes. Recognition levels – affinity, specificity and selectivity. Molecular recognition and its evolution.
- Energetic analysis of biomolecular interactions: Molecular Mechanics, introduction to ab-initio protein folding, Empirical energy functions and Force Fields, Energy Minimization algorithms, Free Energy Surfaces, Molecular Dynamics, Enthalpic and Entropic terms.
- Subcellular Location and protein translocation: endoplasmic reticulum and its functions, ligand binding, target recognition and signal transduction
- Protein folding – molecular chaperones: new viewpoints and theories for protein folding and organization. The importance of topology. Chaperone proteins.
- Biological membranes and membrane proteins: expression, purification and structure determination. Membrane protein structure and function, Membrane protein classifications, Ion channels and receptors, α-helical transmembrane proteins and transmembrane β-barrels
- Drug design: methods for drug design, target based screening and challenges; drug resistant diseases and cancer
- Signal transduction: mechanisms for signal transduction, hormones, neurotransmitters, second molecule messengers. Signal transduction in the membrane and cell interior. Steroids and their receptors, pheromones, G-protein coupled receptors etc.
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Administrator
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Ελληνικά