85304 - Structural Biology

Academic Year 2022/2023

  • Moduli: Maria Paola Turina (Modulo 1) Luisa Iommarini (Modulo 2) Luisa Iommarini (Modulo 3)
  • Teaching Mode: Traditional lectures (Modulo 1) Traditional lectures (Modulo 2) Traditional lectures (Modulo 3)
  • Campus: Bologna
  • Corso: First cycle degree programme (L) in Genomics (cod. 9211)

Learning outcomes

By the end of the course the student is provided with basic knowledge pertaining X-ray crystallography, NMR and cryoelectron microscopy applied to the structural characterization of proteins and nucleic acids. By the end of the hands-on lab the student is able to use programs for the interactive visualization and analysis of molecular structures and related data.

Course contents

Module 1 (3 ECTS, 24 hrs, teacher: Prof. M. Paola Turina)

  • Elements of protein structure and protein folding.
  • Overview of the experimental methods applied to obtain the structure at atomic resolution of proteins and nucleic acids: X-ray crystallography, NMR spectroscopy, Cryoelectron Microscopy.
  • Use of Molecular Visualization software.

Module 2 (3 ECTS, 24 hrs, teacher: Prof. Luisa Iommarini)

Examples of applications of structural data for the study of protein function, including catalytic mechanisms, in some fundamental cellular processes:

  • Control of cell cycle, mechanisms of regulation of proteins involved in cell cycle.
  • Intracellular signalling (G-protein coupled receptors, RTK, nuclear receptors.
  • Proteins involved in ATP production (structural arrangement of OXPHOS complexes and super-complexes, and thier catalytic mechanisms.

Module 3 (2 ECTS, 30 hrs, practical lab, teacher: Prof. Luisa Iommarini)

  • Sample preparation for denaturing polyacrylamide gel electrophoresis SDS-PAGE: lysis of bovine heart mitochondria and protein dosage.
  • Mitochondria of bovine heart lysates separation by SDS-PAGE and OXPHOS subunits visualisation by Western Blotting.
  • Native solubilisation of oxidative phosphorylation complexes from bovine heart mitochondria and protein dosage. SDS-PAGE results analysis.
  • Native solubilisation of respiratory chain super-complexes from bovine heart mitochondria and protein dosage.
  • Blue-Native polyacrylamide gel electrophoresis (BN-PAGE) and in gel activity (IGA) of complexes/super-complexes.
  • Analysis of experimental results.

Readings/Bibliography

Selected reviews, scientific articles and book chapters will be provided. This material will be available for student's use only on the webpage of the course (https://virtuale.unibo.it/)

Teaching methods

Modules 1 and 2: Teacher lectures and student involvement in PC-based activities.

Module 3: Hands-on lab activities, assisted by introductory lectures and tutorials (some lectures will be given just on-line).

 

In consideration of the types of activities and teaching methods adopted, the attendance of this training activity requires the performance of all students of modules 1 and 2 in e-learning mode [https://www.unibo.it/it/servizi-e-opportunita/salute-e-assistenza/salute-e-sicurezza/sicurezza-e-salute-nei-luoghi-di-studio-e-tirocinio] and participation in module 3 of specific training on safety and health in the places of study. Information on dates and methods of attendance of module 3 can be consulted in the specific section of the degree program website.

Assessment methods

Written test and oral interview. The written test will consist of a few open-ended questions and a few multiple-choice questions. The oral interview (if requested by the student) will discuss the written test. The weighted average will be given by the final grade in Structural Biology and Multiscale Modelling. Verbalization will be provided by Prof. Matteo Masetti.

Teaching tools

Videoprojector, PC, internet. Lecture slides will be available.

Office hours

See the website of Luisa Iommarini

See the website of Maria Paola Turina

SDGs

Good health and well-being Quality education

This teaching activity contributes to the achievement of the Sustainable Development Goals of the UN 2030 Agenda.