BIOCHEMISTRY (C)
cod. 1002296

Academic year 2022/23
1° year of course - Second semester
Professor
- Elena FERRARI
Academic discipline
Biochimica (BIO/10)
Field
Attività formative affini o integrative
Type of training activity
Related/supplementary
20 hours
of face-to-face activities
2 credits
hub: PARMA
course unit
in ITALIAN

Integrated course unit module: BIOCHEMISTRY AND MOLECULAR BIOLOGY

Learning objectives

Knowing how to describe and comment on structural properties of globular and fibrous proteins; to understand the folding process, the concepts of misfold and protein aggregation. Knowing and knowing how to explain the cellular processes related to protein homeostasis.
Knowing how to describe and comment on structure, function, mechanism of action and deficiency syndromes of water-soluble vitamins.

Prerequisites

Course unit content

Protein structure, protein folding and folding models. Protein homeostasis: post-translational modifications, targeting and quality control of folding. Protein misfolding and aggregation.
Water-soluble vitamins: structure, function, mechanism of action and deficiency syndromes.

Full programme

Protein structure - Peptide bond: planarity, configuration, rigidity and rotations. Peptides and proteins, detailed description of protein structure levels.
Motifs and structural domains - Definitions of structural motif and domain. Examples of motifs and domains of alpha, beta and alpha / beta type. Multiple domain proteins.
Fibrous proteins – Keratin and collagen: structural and functional aspects. Collagen diseases. Structural elements of Immunoglobulin G. Structural features of membrane proteins.
Protein homeostasis - Post-translational modifications, protein targeting to nucleus, mitochondria, endoplasmic reticulum; secretory pathway, localization in lysosome and cell membrane.
Protein folding - Thermodynamics and folding, Anfinsen experiment, Levinthal paradox, folding models, energy landscape model.
Protein homeostasis - Folding quality control: disulfide isomerase protein, peptidylprolyl cis /trans isomerase, molecular chaperones, chaperonin, unfolded protein response.
Protein degradation mediated by lysosome and ubiquitin-proteasome system.
Protein misfolding and aggregation - Conformational diseases, amyloid fiber: cross-beta structure, aggregation, growth and propagation mechanisms. Prions and conformal contagion.

Water-soluble vitamins, B-complex and vitamin C:
- structural formula
- natural sources
- biological action, mechanism of action of the coenzymatic form
- recommended daily intake levels
- deficiency syndrome

Bibliography

Nelson DL, Cox MM: I principi di Biochimica di Lehninger, Zanichelli, Bologna.
Voet D, Voet JG: Biochimica John Wiley & Sons, USA.
L. Pollegioni: Fondamenti di Biochimica, EDISES.

Teaching methods

The course will be held through lectures to the students in classroom. Lessons will be aided by presentations and videos, promoting the molecular approach to the topics; web sites and references of interest will be suggested.
Lectures will be supported by slide presentations, which will be available to the students on Elly platform (https://elly2022.medicina.unipr.it/).

Assessment methods and criteria

The exam consists in a written test with closed answers, made of 30 multiple-choice questions, ten of which concerning the Biochemistry of Proteins and water-soluble Vitamins. Time allotted for the test is 60 minutes; in the first 20 minutes, the students are allowed to quit, returning the test to the commission. Each positive answer contributes with 1 point to the final grade (0-30/30). There is no penalty for incorrect answers. In case of a positive result, you can choose whether to proceed with the recording of the grade or to take an oral exam.
Students with SLD / BSE must first contact Le Eli-che: support for students with disabilities, D.S.A., B.E.S. (https://sea.unipr.it/it/servizi/le-eli-che-supporto-studenti-con-disabilita-dsa-bes).

Other information