STRUCTURAL BIOLOGY AND NANOTECHNOLOGY (WITH LABORATORY)
4 credits during the 1st year of 9018 Chemical Sciences (LM-54) GENOVA
4 credits during the 2nd year of 9018 Chemical Sciences (LM-54) GENOVA
The course is structured in two modules: Structural Biology and Nanotechnologies
The structural Biology module is aimed at students of the postgraduate courses of Biotechnology, Biological Sciences, Chemistry, Materials Sciences.
The course consist of two modules: Structural Biology and Nanotechnology. The Structural Biology module aims to provide the basis for understanding the three-dimensional structure of macromolecules of biochemical and biotechnological interest such as proteins and nucleic acids. The functional aspects to structural ones will be discussed through various examples present in the literature. The Nanotechnology module aims to provide students with an overview of the latest and most advanced nanobiotechnologies and nanobiomaterials. In particular, the two aspects of nanobioscience and nanobiotechnology application take place: structural proteomics and functional proteomics. In the first case, the novel method of protein nanocrystallography and the advanced synchrotron radiation techniques, including micro and nano-focussed high intense synchrotron radiation and the new trends in radiation damage reduction are presented. In the second case, the most innovative technologies of protein microarrays NAPPA (Nucleic Acid Programmable protein Array) and their fluorescent-label as well as label-free technology of are demonstrated. In the both cases the application to the regenerative medicine are underlined.
AIMS AND LEARNING OUTCOMES
The Structural Biology module aims to provide the basis for understanding the three-dimensional structure of macromolecules of biochemical and biotechnological interest such as proteins and nucleic acids. The functional aspects to structural ones will be discussed through various examples present in the literature.
Frontal lessons. Laboratory exercises
Chemical bonds that stabilize polypeptides: covalent bonds (peptide bond and its properties), hydrogen bonds, salt bridges, hydrophobic bonds, and weak electrostatic interactions. Molecular structures, and their stability. Main classes of organic organic molecules and basis of nucleic acids and proteins structures. Structure of nucleic acids. Primary and secondary structure of DNA and RNA and their integration into the genome. Tertiary structure of tRNA and rRNA. Methods for the definition of the primary structure of nucleic acids. Quaternary structure of the ribosome (rRNA protein integration). Structure of human chromosomes. Protein structure and function. Methods for studing the primary protein structure; Edman degradation, electrospray mass spectrometry, and single or multiple analyzers (MS / MS) MALDI. Levels of structural organization of proteins (primary, secondary, tertiary and quaternary structures). Motifs and domains. Dynamic and thermodynamic folding processes. Molecular evolution, conservation of the three-dimensional fold (divergent evolution, convergent evolution) and protein topologies. Classification of protein structure in structural hierarchies with increasing detail. Correlation of structures with the biological activity of proteins (examples of literature). Principles of crystallization and analysis of crystals of biological macromolecules. Hydrodynamic principles and models for the study of low resolution proteins. Protein Representative Graphing Methods: Lesk & Hardman, RIBBON, TOPS. Van der Waals surfaces. Protein surfaces and interactions with other proteins, ligands and nucleic acids. Criteria for the recognition of binding sites and catalysis. Catalysis and enzymatic kinetics: mechanisms of action of some classes of enzymes of biotechnological and biomedical interest.
Protein structure and function - Petsko G. A.; Ringe D. – Zanichelli
Introduction to Protein Structure - Branden C., Tooze J. - Garland Pub
Ricevimento: By appointment by email: firstname.lastname@example.org
GIANLUCA DAMONTE (President)
ALBERTO GIOVANNI DIASPRO (President)
PIER PAOLO POMPA
Frontal lessons. Laboratory exercises
March 1st, 2019
Oral exam lasting about 30-40 minutes / student on the topics covered in class.
Usually the student is asked three questions of increasing difficulty aimed at assessing the degree and the preparation of the student.
Assessment of the knowledge of: structure and function of proteins, mechanisms of enzymatic catalysis , structure and function of nucleic acids