OVERVIEW

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.

AIMS AND CONTENT

LEARNING OUTCOMES

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.

TEACHING METHODS

Frontal lessons. Laboratory exercises

SYLLABUS/CONTENT

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.

RECOMMENDED READING/BIBLIOGRAPHY

Protein structure and function - Petsko G. A.; Ringe D. – Zanichelli

Introduction to Protein Structure - Branden C., Tooze J. - Garland Pub

TEACHERS AND EXAM BOARD

Exam Board

GIANLUCA DAMONTE (President)

ALBERTO GIOVANNI DIASPRO (President)

ENRICO MILLO

PIER PAOLO POMPA

ANNALISA SALIS

LESSONS

LESSONS START

March 1st, 2019

Class schedule

The timetable for this course is available here: Portale EasyAcademy

EXAMS

EXAM DESCRIPTION

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 METHODS

Assessment of the knowledge of: structure and function of proteins, mechanisms of enzymatic catalysis , structure and function of nucleic acids

Exam schedule