STRUCTURAL BIOCHEMISTRY

The first part of the course covers the study of the chemical and physical properties of amino acids, peptides and proteins. Specific lectures are dedicated to the folding and unfolding of proteins and to the techniques to monitor the protein structure and folding, such as circular dichroism, fluorescence, FT-Infrared spectroscopy and biocrystallography. Topics regarding the interactions responsible for structure and stability of proteins, the mechanisms of molecular recognition and interactions between proteins are also covered. The recently discovered intrinsically disordered proteins and misfolded proteins, responsible of severe diseases, are discussed in detail. The turnover and mechanisms of proteolysis of proteins is also considered. Specific classes of proteins such as membrane proteins and proteins involved into transport are finally analyzed in relation to their structure and dynamics.
Detailed program
1. Protein primary structure
2. Protein secondary structure
3. Protein tertiary structure
4. Concept of fold, domain
5. Protein quaternary structure
6. Chemical bonds and short/long interactions
7. Protein Folding, Unfolding and Misfolding
8. Protein denaturation
9. Natively unfolded proteins
10.Protein-protein interaction and protein complex
11.Membrane protein
12.Transport across membranes, Endocytosis and involved proteins
13.Spectroscopy and determination of protein structure
14.Fluorescence: theory and applications
15.Circular dichroism: theory and applications
16. Infrared spectroscopy: theory and applications
17. X Ray and biocrystallography
18. Plasmon surface resonance