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Lingua Insegnamento

Informazioni aggiuntive

Course Curriculum CFU Length(h)


1. Knowledge and understanding:
The aim of the course is the understanding of the molecular basis of biological systems, and of the biochemical mechanisms that regulate the cellular metabolic activities by the knowledge of:
- structure, properties, function, interactions and metabolic reactions of the bio-molecules;
- functionality and regulation of the enzymes;
- production and maintenance of the energy.
- Fundamental principles of biochemical methodologies of separation and characterization of the main classes of the biomolecules, especially proteins.

2. Applying knowledge and understanding:
To write structures of the main classes of biomolecules; to interpret the titration curves of amino acids and deduce acid/base properties of peptides/proteins; to interpret and elaborate binding curves, such as that of the respiratory proteins, and enzymatic kinetic (Michaelis/Menten; allosteric enzymes); to apply knowledge and understanding of structures, chemical bonds and properties of the biomolecules to study metabolic reaction mechanisms; to elaborate and integrate the different metabolic pathways in a unique view. To apply the theoretical knowledges on the biochemical methodologies on practical laboratory activity, in order to develop a correct scientific approach by a molecular point of view.

3. Making judgements: learning the fundamental concepts of Biochemistry will consolidate the student scientific culture and therefore it will allow the autonomous making judgements for the interpretation of the experimental data and in the deepening of their knowledge both in their work area and outside it. Application of the acquired knowledges develops in the students discreet critical skills in molecular issues and the development of interesting analytical capabilities for the results that can be applied in various professional.

4. Communication skills: Acquisition of the ability to expose and explain in a simple but rigorous manner and with the appropriate technical language the molecular processes underlying the living systems.

5. Learning skills: Acquisition of the ability to connect and integrate the knowledge learned from those provided in the previous and subsequent courses.


To attend the lessons it is essential that the student has acquired the knowledge of the basic principles of General and Inorganic Chemistry, Animal and Plant Biology. It is important to know the basics of analytical chemistry.
Prerequisites: To take the exam, the student must have already taken the exams of General and Inorganic Chemistry, Animal and Plant Biology and must have regularly attended the lectures of Organic Chemistry 1.


Structures: 28 hours
-Amino acids. Structure and stereochemistry. Classification. Acid-base properties: Titration curve, pKa, isoelectric point.
-Peptides and Proteins. Characteristics and properties of the peptide bond. Ionization of the peptides/proteins. Structural organization of the proteins. Helix structures, beta sheets and beta turns. Fibrous proteins, collagen biosynthesis and structure. Tertiary structure and globular proteins. Polymeric proteins.
-Hemoproteins. The heme moiety and the Oxygen binding of Myoglobin and hemoglobin, oxygen binding curve. Allosteric properties of the hemoglobin, modulators of the oxygen binding. The gas transport.
-Carbohydrates. Nomenclature. Stereochemistry. The hemiacetals anomeric forms. Derivatives of sugars. Glycosidic bonds. Disaccharides and polysaccharides. Structure of amylose, amylopectin, glycogen and cellulose.
-Nucleotides and nucleic acids. The purinic and pyrimidinic bases. The nucleotides. Structure of DNA and RNA, properties and biological role.
-Lipids. Classification, glycerophospholipids, sphingolipids, cholesterol. Structure and functions. The biological membranes.
Enzymes and Bioenergetics: 20 hours
-Enzymes. Classification and properties of enzymes. The kinetic of enzymes. Factors modifying the enzymatic rate. Significance of Km, Vmax and Kcat. Irreversible and reversible Inhibitors. The Michaelis-Menten equation and the interpretation of the graphics. Double reciprocal plot. Mechanisms of enzyme catalysis, examples. Regulation of the enzyme activity in vivo.
-Vitamins. Hydrosoluble vitamins, their co-enzymatic derivatives, how they work in the metabolic reactions.
-Bioenergetics. Thermodynamic of biological reactions. deltaG, deltaG0 and Keq. Compounds with high hydrolysis energy, phosphorylation at the substrate level and ATP cycle.
Metabolism: 20 hours
-Oxidative phosphorylation. The respiratory mitochondrial chain, its components and their organization. The chemiosmotic theory. ATP synthesis.
-Glucidic metabolism. Glycolysis and its regulation. Fermentation. Metabolism of the pyruvate. Gluconeogenesis. Biosynthesis and degradation of the glycogen. Hormonal control of glucidic metabolism. The pentose-phosphates cycle. Krebs cycle. Chemicals reactions and their metabolic regulation.
-Metabolism of lipids. Mobilization of fatty acids. beta-oxidation, hormonal and metabolic regulation. Ketogenesis. Biosynthesis of fatty acids.
-Metabolism of amino acids. Metabolic role of amino acids. Catabolism of amino acids. Transamination, deamination, decarbossilation. Urea cycle.

-Strategies for protein purification. Salting out, organic solvents and isoelectric precipitations.
-Chromatographic techniques: Matrices, stationary and mobile phases. Low-pressure column chromatographic systems: ion-exchange, molecular exclusion, hydrophobic interactions and affinity chromatography. High pressure chromatographic systems (HPLC): reverse phase chromatography.
-Electrophoretic Techniques: Zonal electrophoresis. Polyacrylamide gel protein electrophoresis under native condition or in the presence of sodium-dodecil-sulfate (SDS-PAGE) Isoelectric focusing (IEF). Bidimensional electrophoresis (2-DE). Colorimetric staining. Electrophoresis on agarose gel. Western blot.
-Spectrophotometry UV/VIS: Lambert-Beer law and quantitative applications. Absorbance spectra. Determination of total protein concentration. Applications for enzymatic dosages. Fluorescence analysis: principles, instruments and applications.
-Characterization of proteins: Determination of protein MW, pI and amino-acid composition. Amino- acid analyzer. Determination of N- and C- terminal residues. Primary structure sequence determination: chemical and enzymatic methods.
-Use of a software to simulate protein purification experiments.

Teaching Methods

Lectures will be prevalently held in classrooms, also integrated with online teaching resources, by using specific online platforms managed by the University of Cagliari.

Teachers provide individual explanations to students during weekly office hours.The course begins in mid-November with the Biochemistry module (6 hours of weekly lesson) and continues in the second semester with the two modules (4 hours of weekly lesson for the Biochemistry module and 4 hours for the Applied Biochemistry module).
For biochemistry module the following classroom activities are scheduled:
total hours of frontal lessons = 68 subdivided in 28 hours on the structure of biomolecules and their biological properties (sugars, lipids, nucleic acids, amino acids and proteins, hemoproteins); 20 hours on enzymology, structure and function of coenzymes and bioenergetics; 20 hours on metabolism.
- 4 hours devoted to written tests that can be evaluated for examination;
- Tutorial activities (by the tutor, in addition to teacher's lectures) consisting in classroom exercises and tutorials to help the student learn the biomolecular structures, acid-base properties of amino acids and peptides, interpretation of oxygen / hemoglobin binding curves, enzymatic kinetics And calculation of ΔG0 in metabolic reactions.
To assist with the study of the General Biochemistry, the teacher provides lecture slides, exercise books and copies of previous written tests.

For the Applied Biochemistry Module:
- 32 hours of classroom lectures
- 12 hours of practical activity in laboratory (with compulsory attendance), carried out with the help of tutors.
- 4 hours of informatic lab tutorial to simulate protein purification experiments in order to develop decisional abilities and critical analysis on the results obtained.

Verification of learning

Biochemistry: Written and oral examination.
For students that have regularly attended lectures, two written tests will be carried out during the course:
1) Structure and acid-base properties of amino acids and peptides; Structure of proteins, sugars, lipids, nucleotides and ac. nucleic; Biological membranes. Respiratory protein properties. Interpretation of binding curves.
2) Environmental kinetics, interpretation of graphs; Catalysis and regulation mechanisms. Coenzymes; DeltaG calculation.
Grades for the written tests will be in thirtieths and considered for the final evaluation, insufficient parts will be verified in the oral test. If the test has got a failing grade, the test must be repeated on on the day of the exam. The student can repeat, on the day of examination, the written tests he believes may be improved.
For non-attending students, on the day of examination, a single written Biochemistry test should be undertaken. In the oral test the student is required to write metabolic reactions, structure of metabolites, mechanism of the most important reactions and discuss their regulation.
Applied Biochemistry: At the end of the course, students who have regularly attended lectures (>75%) may undertake a written report (2 CFU) on protein purification using a simulation software to demonstrate their knowledge in using both analytical and preparative separation techniques. If the report is well-done, the grades will be weighted with those of the oral exam (3 CFUs), which will focus on topics not discussed in the test. Students who do not take the end-of-course examination, or those who do not perform well, will take an oral exam on the entire program (5 CFUs).

The total score, in thirtieths, is the result of the weighted grades of the two modules (9 + 5 CFU). Here is a list of the conditions that should be verified during the exam for assigning the relative grades:
• 30 cum laude: excellent knowledge of all subjects, accurate, detailed and enriched critical and personal points of view, ability to describe an overview of metabolic processes, excellent communicative ability, broad judgment autonomy, and learning abilities.
• 30: Acquire all the required knowledge, ability to apply them to the resolution of analytic problems proposed in the exams. Precise and impeccable oral exposure to language skills and communicative skills, judgmental autonomy and excellent learning skills.
• 27-29: Acquisition of all required knowledge, ability to solve analytic problems. Exposure to the correct but not detailed or inaccurate arguments. Autonomy of judgment, communication skills and good and appropriate learning skills.
• 25-26: Acquiring the knowledge required and ability to use them in the processing of biochemical topics, albeit with slight gaps, fluid but imprecise exposure. Autonomy of judgment, communicative abilities and discrete learning abilities.
• 22-24: poor acquisition of required knowledge, skills in imprecise and incomplete arguments. Errors in writing structure and ties. Adequate communication skills, autonomy of judgment and appropriate learning skills, even with some uncertainty.
• 18-21: acquiring the minimum knowledge on the topics studied, allowing them to write the structure of the most important biomolecules and to argue the basics of enzymatic kinetics, metabolism, and the main techniques of purification and characterization of proteins. Difficulties in solving the proposed analytic problems. Poor language skills and communication skills, skills, judgment autonomy, and just as much learning ability as a whole.


for the Biochemistry module (with a choice between):
-FONDAMENTI DI BIOCHIMICA di D. Voet, JG. Voet, CW Pratt. Ed. ZANICHELLI. Quarta Edizione, 2017.
-I PRINCIPI DI BIOCHIMICA DI LEHNINGER di D.L. Nelson, M.M. Cox. Ed. ZANICHELLI. Settima Edizione, 2018.
-PRINCIPI DI BIOCHIMICA. Horton, Moran, Scrimgeour, Perry, Rawn. Ed. Pearson. Quarta Ed.

for the Applied Biochemistry module.
Metodologie Biochimiche. Bonaccorsi, Contestabile, Di Salvo. II ed. Zanichelli, 2019

More Information

Biochemistry: Lesson slides and exercises will be provided in PDF format

Questionnaire and social

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