Unit PROTEIN BIOTECHNOLOGY
- Course
- Molecular and industrial biotechnology
- Study-unit Code
- A003308
- Curriculum
- In all curricula
- Teacher
- Lorena Urbanelli
- Teachers
-
- Lorena Urbanelli
- Hours
- 47 ore - Lorena Urbanelli
- CFU
- 6
- Course Regulation
- Coorte 2023
- Offered
- 2023/24
- Learning activities
- Caratterizzante
- Area
- Discipline biologiche
- Academic discipline
- BIO/10
- Type of study-unit
- Obbligatorio (Required)
- Type of learning activities
- Attività formativa monodisciplinare
- Language of instruction
- Italian
- Contents
- From sequence to structure: basic principles of protein structure
From structure to protein function: enzymatic catalysis and examples of catalytic mechanisms. Control of protein function: mechanisms of inhibition and regulation of enzymatic activity. Methods for measuring enzyme activity.
Membrane proteins: structural and functional aspects
fibrous proteins
Vectors and hosts for the production of recombinant proteins in prokaryotes
Vectors and hosts for the production of recombinant proteins in eukaryotes
Targeted mutagenesis and protein optimization
Examples of recombinant protein production and industrial applications of enzymes.
Protein purification strategies
Topics that will be developed in the laboratory:
Expression of a eukaryotic protein in mammalian cells
Application of a protein purification strategy - Reference texts
- Petsko-Ringe Struttura e funzione delle proteine, Zanichelli
- Educational objectives
- The main objective of the course is to provide students with a good understanding of the structural and functional characteristics of proteins, their methods of production, purification and optimization, as well as their potential applications in the various biotechnological sectors. The knowledge acquired will allow the student to understand the different modes of action and critically evaluate the parameters that can influence their activity in order to be able to predict possible applications in the various biotechnological sectors, with particular regard to the industrial sector. The practical exercises will provide the student with the necessary tools to apply the theoretical knowledge acquired in order to solve problems and design experiments.
- Prerequisites
- To understand and profitably attend the course, it is useful for the student to have a good knowledge of basic elements of general and inorganic chemistry, organic chemistry and biochemistry
- Teaching methods
- The course is organized as follows:
- lectures in the classroom related to the topics covered by the program. Lessons will be carried out with the aid of slide projections and films;
- final seminar of each student with the presentation of a case study of the production of a protein;
- practical activity in the laboratory. The students will be divided into groups of 3-4 students per group and will personally carry out the analyses foreseen in the course programme. The practical part will be preceded by an introduction in the classroom. During the exercises the students will be assisted by expert and qualified laboratory personnel. - Other information
- For the calendar of teaching activities and the start and end dates of the lessons, please consult the degree course website: http://www.dcbb.unipg.it/laurea-magistrale-in-biotecnologie-molecolari-e-industriali
- Learning verification modality
- The exam includes a 15-minute seminar test which consists in the presentation of a case study about the production of a protein and an oral test which consists in a discussion relating to the topics covered during the course. The duration of the exam may vary depending on the progress of the test itself, with an average duration of about 30-40 minutes in total. The oral exam aims to evaluate the level of knowledge and understanding achieved by the student regarding the topics covered. Furthermore, this interview will make it possible to verify the student's ability to communicate with language properties and clarity of exposition what has been learned
- Extended program
- From sequence to structure: amino acids, peptide bond. Importance and determinants of secondary structure. Properties of alpha helices and beta sheets. Folding and tertiary structure. Determinants of tertiary structure: stability, flexibility, post-translational modifications. Protein motifs: alpha motifs and beta motifs. Mixed motifs.
From structure to function of proteins: ligands, binding sites. Enzymatic catalysis, enzyme kinetics, examples of catalytic mechanisms. Active site geometry and transition state. Examples of reactions: redox, hydrolysis, decarboxylation
Control of protein function: mechanisms of inhibition and regulation of enzymatic activity. Cooperative binding, competitiveness, conformational changes and allostery. Interaction between proteins, regulation by localization, control of pH and redox environment. Methods of measurement of enzyme activity. Regulation by degradation and by phosphorylation.
Vectors and hosts to produce recombinant proteins in prokaryotes. Vectors and hosts to produce recombinant proteins in eukaryotes. Targeted mutagenesis and protein optimization. Protein purification strategies. Examples of recombinant protein production and industrial applications of enzymes.