ID:
506610
Duration (hours):
48
CFU:
6
SSD:
BIOLOGIA MOLECOLARE
Year:
2025
Overview
Date/time interval
Secondo Semestre (02/03/2026 - 12/06/2026)
Syllabus
Course Objectives
The aim is to provide in-depth knowledge in the study of proteins and macromolecular complexes underlying biological processes, with particular attention to methods for determining their biochemical and structural characteristics and related biotechnological applications. The aim is also to enable the student to understand the scientific articles concerning the study of proteins and to apply the methods described, including those for visualizing the structures, to obtain useful information in future working contexts.
Course Prerequisites
The course deals with topics and methods of Molecular Biology and Biochemistry at advanced level. Therefore, a basic knowledge of these subjects is fundamental.
Teaching Methods
Lectures possibly integrated with seminars. Interactive teaching methods (like article reading, computer-based tools with real-time feedback etc.) may be used to improve learning and student participation). No practicals in the lab are included.
Assessment Methods
Oral exam that will verify the acquired knowledge of the topics but also the quality of presentation and the usage of the correct language and terminology.
Texts
“Physical Biochemistry: principles and applications”, David Sheehan, Wiley-Blackwell – 2nd edition
Contents
In particular, the course will comprise the following topics:
Biological function of proteins and their chemical properties. Protein structure: primary, secondary, tertiary, quaternary structure. The problem of the mechanism of protein folding. Role of chaperones. Peculiar cases of folding: eukaryotic proteins, membrane proteins, intrinsically disordered proteins. Biotechnology applications of studying protein structure: analysis of protein-protein interactions and protein-ligand, biocatalysis and enzymes for industrial interest, drug design. Production of recombinant proteins for structural biology. Protein purification by advanced chromatographic methods, Protein Data Bank (PDB) and bioinformatics tools for protein engineering.
Methods for studying the structure of macromolecules. Nuclear Magnetic Resonance (NMR): the magnetic spin moment, the Larmor frequency and the resonance conditions; 1D NMR spectra and multidimensional NMR; examples of structures determined with NMR. X-ray crystallography: crystallization of macromolecules and properties of crystals; theory of X-ray diffraction and experimental methods for data collection; amplitude and phase of diffracted rays and structure factors; analysis of the electron density map and modelling of protein polypeptide chain; examples of structures solved by X-ray crystallography. Electron microscopy: TEM and SEM; Cryo-EM; sample preparation and negative stain; single-particle EM, 3D reconstruction from 2D projections; examples of structures determined by EM.
Complementary methods for the study of biomolecules and their biotechnological applications: Surface Plasmon Resonance (SPR), Isothermal Titration Calorimetry (ITC), Microscale Thermophoresis
Biological function of proteins and their chemical properties. Protein structure: primary, secondary, tertiary, quaternary structure. The problem of the mechanism of protein folding. Role of chaperones. Peculiar cases of folding: eukaryotic proteins, membrane proteins, intrinsically disordered proteins. Biotechnology applications of studying protein structure: analysis of protein-protein interactions and protein-ligand, biocatalysis and enzymes for industrial interest, drug design. Production of recombinant proteins for structural biology. Protein purification by advanced chromatographic methods, Protein Data Bank (PDB) and bioinformatics tools for protein engineering.
Methods for studying the structure of macromolecules. Nuclear Magnetic Resonance (NMR): the magnetic spin moment, the Larmor frequency and the resonance conditions; 1D NMR spectra and multidimensional NMR; examples of structures determined with NMR. X-ray crystallography: crystallization of macromolecules and properties of crystals; theory of X-ray diffraction and experimental methods for data collection; amplitude and phase of diffracted rays and structure factors; analysis of the electron density map and modelling of protein polypeptide chain; examples of structures solved by X-ray crystallography. Electron microscopy: TEM and SEM; Cryo-EM; sample preparation and negative stain; single-particle EM, 3D reconstruction from 2D projections; examples of structures determined by EM.
Complementary methods for the study of biomolecules and their biotechnological applications: Surface Plasmon Resonance (SPR), Isothermal Titration Calorimetry (ITC), Microscale Thermophoresis
Course Language
Italian
More information
For students who certify that they are in one of the categories indicated by the University (disabled, workers, etc.) the teachers will be able to provide support based on what is indicated by the University, or through meetings for clarifications on certain topics of the course and possibly providing the corresponding videotapes of lessons from past years that include those specific topics.
Degrees
Degrees
ADVANCED BIOTECHNOLOGY
Master’s Degree
2 years
No Results Found
People
People
No Results Found