Structure, Biosynthesis and Analysis of Proteins

Course objectives

General aims This course aims to lead students to a deeper knowledge on folds and folding of proteins and protein complexes, to enable them to present/disseminate/discuss specific protein structure-function relationships, and to introduce them to current knowledge on "molecular machines”. Specific aims • Preliminary knowledge Basic notions of protein structure (indispensable), molecular biology (indispensable), genetics (important) and cellular biology (important) • Knowledge of the student at the end of the course: Students will acquire knowledge of the complex dynamic events that bring the newly formed polypeptides to assume 3D structures and biological functions, and will familiarize with the main methodologies in protein structure determination. • Acquired skills of the student with this course: At the end of the course, students will be able to query protein 3D databases, and to create publication quality images and movies by molecular graphics. • Critical and judgmental skills acquired at the end of the course: Students will know how to discuss in depth structure-function relationships of specific proteins, to interpret in a structural key the biological consequences of genetic mutations, and to address the design of modified protein structures. • Communication skills on course content: The final assessment intends to evaluate acquired knowledge, but also student skills in the use of molecular graphic programs, both in research and in result dissemination. • Ability to continue independently From the knowledge of the addressed topics, students will have acquired the cultural background and the prerequisite skills to face a wide range of Protein Biochemistry issues.

Channel 1
MARTINO LUIGI DI SALVO Lecturers' profile

Program - Frequency - Exams

Course program
Amino Acids - physico-chemical properties and structure Visualizing Macromolecules with molecular viewers Protein Sequence Databases Protein Sequence Alignments The Peptide Bond in vitro and in Vivo Secondary Structure Tertiary Structure - Protein Stability and Folding Domains, Motifs, Modules and Repeats - Quaternary Structure Electron Microscopy and X-ray crystallography Nuclear Magnetic Resonance of Proteins Protein Structure Prediction Molecular Dynamics and Drug Design Selected examples of Protein mechanisms
Prerequisites
In general, students taking this course should have a basic knowledge of biochemistry and molecular biology. More specifically, students are expected to have foundational knowledge of protein biochemistry (essential), structural molecular biology (essential), genetics (important), and cell biology (important).
Books
- C. I. Branden, J. Tooze. Introduction to protein structure - Garland Science - David Whitford, PROTEINS STRUCTURE AND FUNCTION (Wiley; http://books.google.it/books?id=qbHLkxbXY4YC) - Voet, Voet, Pratt - Fundamentals of Biochemistry: Life at the Molecular Level - Wiley) - Petsko & Ringe - Protein Structure and Function - OUP Oxford
Frequency
Not mandatory
Exam mode
Original presentation of the structure–function relationship of a chosen protein system using molecular graphics, including: - The description of the levels of structural organization (domain organization, topological aspects and connectivity between secondary structure elements, structural motifs and fold) and, where available, aspects of the folding process; - An in-depth analysis at the amino acid level of a specific detail of the structure–function relationship; - Evolutionary and applicative considerations. The discussion on the chosen topic will place particular emphasis on the methodological approach. The assessment also includes an oral exam in which all parts of the program will be discussed
Lesson mode
The course combines traditional lectures with interactive and practical activities. Lectures will cover the core topics of the program through instructor-led explanations, supported by slides, extensive board work, and targeted audiovisual materials to deepen understanding of specific subjects. Certain topics will be further explored in specialized seminars led by professors and researchers with extensive expertise in the field. Active interaction between instructors and students is a central element of each session. Open discussions on lecture topics encourage students to participate and engage with one another, fostering communication, critical thinking, and analytical skills. The methodological component is addressed through bioinformatics laboratory exercises, video analyses of experimental studies, the design of original experimental setups, simulation of potential outcomes, practical laboratory verification, and discussion of the results. This integrated approach ensures both theoretical understanding and hands-on experience in protein structure and analysis.
ELENA FORTE Lecturers' profile
  • Lesson code1051868
  • Academic year2025/2026
  • CourseGenetics and Molecular Biology
  • CurriculumGenetics and Molecular Biology (percorso valido anche ai fini del conseguimento del doppio titolo italo-francese) - in lingua inglese
  • Year1st year
  • Semester1st semester
  • SSDBIO/10
  • CFU6