First cycle
degree courses
Second cycle
degree courses
Single cycle
degree courses
School of Science
Course unit
SCP4067771, A.A. 2019/20

Information concerning the students who enrolled in A.Y. 2019/20

Information on the course unit
Degree course First cycle degree in
SC1165, Degree course structure A.Y. 2008/09, A.Y. 2019/20
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Number of ECTS credits allocated 7.0
Type of assessment Mark
Course unit English denomination BIOCHEMISTRY I
Website of the academic structure
Department of reference Department of Biology
Mandatory attendance
Language of instruction Italian

Teacher in charge MARISA BRINI BIO/10
Other lecturers ELENA ZIVIANI BIO/10

Integrated course for this unit
Course unit code Course unit name Teacher in charge

ECTS: details
Type Scientific-Disciplinary Sector Credits allocated
Basic courses BIO/10 Biochemistry 7.0

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

Type of hours Credits Teaching
Hours of
Individual study
Laboratory 1.0 16 9.0 3
Lecture 6.0 48 102.0 No turn

Start of activities 02/03/2020
End of activities 12/06/2020
Show course schedule 2019/20 Reg.2008 course timetable

Examination board
Examination board not defined


Common characteristics of the Integrated Course unit

Prerequisites: Basic knowledge of inorganic and organic chemistry
Target skills and knowledge: The student will be familiar with cellular and whole-organism metabolism and will acquire the information necessary to understand cellular biology and physiology classes.
Examination methods: Written examination with both multiple choice and open questions
Assessment criteria: The student has to provide evidence of having understood and studied the information given during the lectures and those found in the textbooks.

Specific characteristics of the Module

Course unit contents: Proteins (2 CFU, 16 hours). Amino acids: structure, properties and classification. Modified amino acids. Structures and properties of the peptide bond. Polypeptides chains. Peptides of biological interest. Levels of structure in protein architecture. Primary structure. Ramachandran plot. Tridimensional structure of the proteins. Secondary structure: alpha-helix, beta-sheet, beta turn. Fibrous proteins (fibroin, keratin, collagen, elastin). Super secondary structures. Tertiary structure. Globular proteins. Structural domains and structure/function relationship. Denaturation. Molecular dynamics of globular proteins. Secondary structure prediction and relationship between primary sequence and tridimensional structure. Protein folding. Quaternary structure.

Oxygen-transporting proteins (0,75 CFU, 6 hours). Myoglobin and hemoglobin. Oxygen binding. Cooperative binding. Allosteric effects and allosteric factors. Bohr effects. Fetal hemoglobin and hemoglobin S.

Enzymes (1CFU, 8 hours). Catalysis and enzyme kinetic. Michaelis–Menten model. Significance of vmax, Km and Kcat and their calculation. Energetic profile of an enzymatic reaction. pH effect in enzymatic catalysis. Regulation of enzymatic activity: inhibition, allosteric regulation, covalent modifications, proteolytic cleavage. Role of coenzymes and metal ions. Catalytic mechanisms: serine proteases.

Carbohydrates (0,75 CFU,6 hours). Monosaccharides, disaccharides and their products. Oligosaccharides. Polysaccharides. Omo- and hetero-polysaccharides. Glycoproteins and glycolipids. Structure and function.

Nucleotides and Nucleic acids (0,25 CFU, 4 hours). Nucleotides and phosphodiester bond. The nature of nucleic acids: RNA, DNA and their primary structure. Secondary structures of DNA: helix A;B and Z. Denaturation of DNA molecules. RNA and its tridimensional structures. ATP, FMN, FAD, NAD+.

Lipids and Biological membranes (1 CFU, 8 hours). Structure and properties of lipids (fatty acids, triglycerides, waxes). Membrane lipids (glycerophospholipids, sphingolipids, glycolipids and cholesterol). Lipophilic vitamins. Structure and properties of the cellular membranes. Fluidity and asymmetry of the membranes. Membrane proteins and their structure. Transport across membranes: mechanisms and classification.

Cell Signalling (0,25 CFU, 4 hours). Examples of molecular mechanisms of signal transduction.

Practicals (1 CFU, 16 hours): Spectrophotometry theory and application. Absorbance spectrum of Flavin mononucleotide (FMN) in oxidized and reduced form. Determination of protein concentration by biuret method. Lactate dehydrogenase activity: experimental determination of vmax and Km values.
Planned learning activities and teaching methods: 48 hours lectures and 16 hours practicals
Additional notes about suggested reading: Slides are available on moodle (

The study on the textbooks is warmly recommended
Textbooks (and optional supplementary readings)
  • RH Garret; CM Grisham, Biochimica. --: Piccin, --. Cerca nel catalogo
  • D.L. Nelson, M.M.Cox, I principi di Biochimica di Lehninger. --: Zanichelli, --. Cerca nel catalogo
  • J.N. Berg,,J.M. Berg, , J.L. Tymoczko, L. Stryer., Biochimica. --: Zanichelli, --. Cerca nel catalogo
  • D. Voet, J.G. Voet, C.W. Pratt., Fondamenti di Biochimica. --: Zanichelli, --. Cerca nel catalogo

Innovative teaching methods: Teaching and learning strategies
  • Laboratory
  • Use of online videos
  • Loading of files and pages (web pages, Moodle, ...)

Innovative teaching methods: Software or applications used
  • Moodle (files, quizzes, workshops, ...)

Sustainable Development Goals (SDGs)
Good Health and Well-Being Quality Education Gender Equality