Medical Biotechnology

Activity type

Discipline biotecnologiche comuni

SSD

BIO/10

Year

N/D

Semester

N/D

CFU

4

Hours distribution

32 classroom hours

Lecturers

Activity type

Discipline biotecnologiche comuni

SSD

BIO/10

Year

N/D

Semester

N/D

CFU

2

Hours distribution

16 classroom hours

Lecturers

CARLO TRAVAGLINI ALLOCATELLI

Activity type

Discipline biotecnologiche comuni

SSD

BIO/11

Year

N/D

Semester

N/D

CFU

3

Hours distribution

24 classroom hours

Lecturers

FRANCESCA CUTRUZZOLA'

Understand the main methodologies for determining protein structures.
Learn the main methods used in proteomic analysis, the types of data generated, and their key limitations.
Determine the thermodynamic stability of proteins and understand their mechanisms of folding. Mechanisms of aggregation and fibrillogenesis. Intermolecular interactions: binding affinity and association/dissociation rate constants.
Learn the general principles of the design, heterologous production and mutagenesis of proteins.
Acquire capacity of critical reading of scientific papers.

Understand the main methodologies for determining protein structures.
Learn the main methods used in proteomic analysis, the types of data generated, and their key limitations.
Determine the thermodynamic stability of proteins and understand their mechanisms of folding. Be able to evaluate the mechanisms of aggregation and fibrillogenesis. Intermolecular interactions: binding affinity and association/dissociation rate constants.
Learn the general principles of the design, heterologous production and mutagenesis of proteins.
Acquire capacity of critical reading of scientific papers.

Basic knowledge of protein structure: chemistry and properties of the peptide bond; structure and names of the 20 amino acids; primary, secondary, tertiary, and quaternary structure of proteins; basic notions of electromagnetic waves and properties of electric and magnetic fields.
Knowledge of the principles of chemical equilibrium, thermodynamics, and kinetics of chemical reactions.
Knowledge of the basic principles of molecular biology of nucleic acids and proteins, including translation and stability in vitro and in vivo. Basic principles of recombinant DNA.

Module: Structural biology and protein engineering I
N/D
Module: Structural biology and protein engineering II
Thermodynamic stability of proteins. Obtaining a denaturation curve by spectroscopic methods at equilibrium. Analysis of a denaturation curve. Protein folding mechanisms. Fast folding kinetics. Characterization of intermediates and transition states. Amyloid fibrils: molecular mechanisms of aggregation and fibrillogenesis.
Inter-molecular recognition. Obtaining and analyzing a binding curve at equilibrium. Binding reactions and kinetic experiments.
Principles of de novo design of artificial proteins.


Module: Structural biology and protein engineering III
Isolation of Protein-coding Genes
Cloning: Classical and Recombinant Methods (GATEWAY/TOPO/CRE-LOX)
Protein Expression: Vectors, Solubility, Tag Use, Cell-Free Expression
Rational Mutagenesis: Classical and PCR Methods
Random Mutagenesis and Guided Evolution
TALEN, ZFN, and CRISPR/CAS Applied to Protein Engineering

Examples of First- and Second-Generation Protein Drugs
Examples of Applications in Biomedicine

Discussion of Aspects Related to Specific Proteins and Nanoparticles
(Articles - See Website)

Module: Structural biology and protein engineering I
N/D
Module: Structural biology and protein engineering II
Slides, notes and relevant scientific papers discussed during the lessons (available on-line to students on the website of the Course).


Module: Structural biology and protein engineering III
Mauro Maccarrone
Metodologie biochimiche e biomolecolari
Strumenti e tecniche per il laboratorio del nuovo millennio

Selected literature reviews will be indicated during the course and on the e-learning platform.

Module: Structural biology and protein engineering I
N/D
Module: Structural biology and protein engineering II
N/D
Module: Structural biology and protein engineering III
N/D

Classroom lessons (mandatory attendance)
Laboratory lessons on selected topics, as indicated above in the program and concerning all parts of the study program.

Mandatory

The exam will be divided in two parts, corresponding to the two semesters. The minimal overall mark for the exam is 18/30.
The written exam includes questions with open answers, as well as multiple choices.
The student must show a basic knowledge of biochemistry, structural biology and molecular biology of proteins, together with the capacity to logically connect and apply this knowledge by solving simple experimental problems.

The questions include multiple-choice questions and open-ended exercises or theoretical questions.

Module: Structural biology and protein engineering I
N/D
Module: Structural biology and protein engineering II

• The topics of the lessons will follow the order of the lessons available online, but are subject to change at the discretion of the teacher.
  • Books:  Slides and other monographic materials provided in class (available on the course e-learning platform)


• Classes take place in the second semester of each academic year.(beginning of March- end of May.The detailed calendar will be published as soon as available.

• The topics of the lessons will follow the order of the lessons available online, but are subject to change at the discretion of the teacher.
  • Books: Mauro Maccarrone
    
    Biochemical and Biomolecular Methodologies (Zanichelli)
    
    Slides and other monographic materials provided in class (available on the course e-learning platform)


• Classes take place in the second semester of each academic year.(beginning of March- end of May.The detailed calendar will be published as soon as available.