OVERVIEW

The course consist of two modules: Biochemistry II and Structural Biology. The Module of Structural Biology is aimed at students in biotechnology, biology, chemistry and materials science.

AIMS AND CONTENT

LEARNING OUTCOMES

"The Structural Biology course 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)

ANNALISA SALIS

LESSONS

LESSONS START

March 1st, 2018

Class schedule

The timetable for this course is available here: Portale EasyAcademy

EXAMS

Exam schedule