First cycle
degree courses
Second cycle
degree courses
Single cycle
degree courses
School of Medicine
Course unit
MEP5070479, A.A. 2017/18

Information concerning the students who enrolled in A.Y. 2017/18

Information on the course unit
Degree course Second cycle degree in
ME2193, Degree course structure A.Y. 2015/16, A.Y. 2017/18
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Number of ECTS credits allocated 6.0
Type of assessment Mark
Course unit English denomination PROTEIN ENGINEERING
Department of reference Department of Pharmaceutical and Pharmacological Sciences
Mandatory attendance
Language of instruction English
Single Course unit The Course unit can be attended under the option Single Course unit attendance
Optional Course unit The Course unit can be chosen as Optional Course unit

Teacher in charge DORIANNA SANDONA' BIO/11

ECTS: details
Type Scientific-Disciplinary Sector Credits allocated
Core courses BIO/10 Biochemistry 6.0

Course unit organization
Period Second semester
Year 1st Year
Teaching method frontal

Type of hours Credits Teaching
Hours of
Individual study
Laboratory 1.0 15 10.0 No turn
Lecture 5.0 40 85.0 No turn

Start of activities 26/02/2018
End of activities 01/06/2018
Show course schedule 2019/20 Reg.2015 course timetable

Examination board
Board From To Members of the board
5 Commissione a.a. 2019/20 02/12/2019 30/09/2020 SANDONA' DORIANNA (Presidente)
4 Commissione a.a. 2017/18 01/12/2017 30/09/2018 SANDONA' DORIANNA (Presidente)

Prerequisites: Students must have a strong background in molecular biology, structural biochemistry and organic chemistry in order to understand the methods of production and modification of proteins and the rationale of the introduced mutations.
Target skills and knowledge: At the end of the course students should:
-know the determinants of protein stability and the rational of the modifications to increase it;
-be able to describe rational and combinatorial methods of protein engineering and the most common mutant selection techniques;
-be able to propose a protein engineering approach to study protein structure and function and to modify and produce a protein for a particular application;
-have acquired the ability to critically analyze literature regarding the application of protein engineering techniques.
Examination methods: Assessment at the end of the course will be based on a written examination consisting of 6 questions (one question related on the practical part of the course) and an oral examination that will comprise also the critical exposition of a recent publication.
Assessment criteria: Assessment at the end of the course aims to test the student's ability:
-to critically describe the main methods used in protein engineering
-to critically describe their applications;
-to be able to design strategies to modify proteins (to increase their stability, to change their specificity toward the substrate, to produce a new function, ect.
-to critically evaluate the literature on protein engineering topics.
Course unit contents: The course deals with molecular biology and chemical methods that are essential to study the structure and function of proteins and to develop proteins with new properties.
The topics covered are as follows:
- chemical stability of proteins and strategies to improve it site
-methods of directed mutagenesis of proteins
-methods of random mutagenesis o proteins
-methodologies to create libraries of mutants (directed evolution) and methods of high-throughput screening
-methods for the production and modification of antibodies, antibody fragments and new binding proteins developed from non-immunoglobulin domains
-circular permutation of proteins
-inteins and their applications
-the chemical synthesis of peptides and proteins
-production of proteins and peptides containing non-natural amino acids.

Example of application in research and in biotechnology industry will be provided in order to better illustrate these techniques.
Planned learning activities and teaching methods: The course consists in class lectures (5 CFU) and a practical part (1 CFU). During the lessons, some hours will be also dedicated to the critical discussion of recent publications that illustrate applications of the methods of protein engineering.
During the practical part, the basic concepts of protein mutagenesis will be summarized and students will perform an experiment of random mutagenesis of the GFP protein by using the error-prone PCR method.
Additional notes about suggested reading: Articles and reviews will be provided to students for home study.
Textbooks (and optional supplementary readings)
  • Sheldon J. Park and Jennifer R. Cochran, Protein Engineering and Design. United States of America: CRC Press, Taylor & Francis Group, 2010. Cerca nel catalogo