Protein engineering and proteomics

A.Y. 2018/2019
Overall hours
Learning objectives
The course provides an introduction to protein
biotechnology and the basic knowledge required for set up
large-scale protein production within biotechnological
industry, from cell cultivation in bioreactors up to protein
purification in a preparative scale and includes different
modern bioanalytical techniques. The course is aimed at
giving students in-depth understanding of 1) the structure-
function relationship of proteins and of 2) the
methodologies used to produce, characterize and use
proteins, enzymes included, and 3) the molecular basis and
protein engineering tools available for designing enzymes
or proteins with new or desirable functions. The course will
have a strong hands-on connotation based on practical
sessions either of experimental design in classroom and of
Expected learning outcomes
At the end of the course the student will be able to
implement the notions of molecular biology, proteomics and
genetic engineering for the production and improvement of
proteins and enzymes. The student will be able to analyze
the structure of proteins and their post-translational
modifications; review the main factors that are significant
for protein folding processes and stability; explain how
proteins can be used for different industrial applications,
carry out mutagenesis approaches to improve protein
stability and to confer on them new functions.
Course syllabus and organization

Single session

Lesson period
Second semester
Course syllabus
Structural/functional molecular characteristics of proteins: from biosynthesis to folding. Structural and functional dynamics of proteins. Modern approaches for the study of the proteins. Implementation of protein purification procedures. Proteome analyses for protein and enzyme identification and exploitation. Recombinant protein technologies; gene expression: vectors, expression in bacteria, yeasts, plants, insect and mammalian cells. Cell-Free translation systems. Inclusion bodies, their solubilization; protein refolding. Co-expression and use of chaperones. Storage stabilization of proteins. Hints of evolutionary biotechnology (rational design and directed evolution). Examples of tailored enzymes in industrial biocatalysis. Production and applications of polyclonal and monoclonal antibodies. Strategies to set up a protein engineering project.
Teaching methods
Reference material (books and relevant scientific papers) will be presented during the first lesson. Slides of the lessons will be available to students through ARIEL platform.
BIO/10 - BIOCHEMISTRY - University credits: 6
Practicals: 16 hours
Laboratories: 8 hours
Lessons: 36 hours
Professor: Scarafoni Alessio
Thursday afternoon only by appointment (by e-mail)
Building 21040, first floor