Elements, biomolecules (functional groups and isomery) and chemical bonds in cell organization and biological phenomena
Water, acids and bases, pH and buffer systems in the human body
Structure, classification, chemical properties and functions. Peptide bond.
Structure (Iaria, IIaria, IIIaria and IVaria), properties and functions. Simple and complex proteins. Structure and functions of:
- fibrous proteins: alpha-keratins, collagen, elastin; biosynthesis of collagen;
- globular proteins: pre-albumin, albumin, immunoglobulins, myoglobin and hemoglobin.
Structure and functions of:
- monosaccharides: aldoses and ketoses, open and cyclic structure, substituted sugars and saccharidic derivatives (aminozuccheri, uronic acids, polyalcohols, desoxizucars, sialic acids); glycosidic bond;
- disaccharides: maltose, isomaltose, lactose, saccharose, cellobiose;
- oligosaccharides: glycoproteins (O-linked and N-linked);
- homopolysaccharides: glycogen, starch, cellulose;
- heteropolysaccharides: glycosaminoglycans (main classes) and proteoglycans.
Structure and functions of:
- saturated and unsaturated fatty acids: nomenclature and numbering);
- triglycerides, glycerolphospholipids, sphingolfospholipids, glycosphingolipids and cholesterol;
- lipid aggregates: micelles, liposomes and plasma lipoproteins.
Composition, structure and properties (asymmetry, fluidity and dynamism). Membrane proteins: structure and functions. Transport mechanisms: simple and facilitated diffusion, active transport, channel proteins, ionophores.
Properties and structural features. Isozymes. Constitutive and inducible enzymes.
Enzymatic kinetics: Michaelis-Menten, Vmax and Km equation; graph of reciprocal doubles.
Regulation of enzyme activity: influence of pH and temperature; inhibition mechanisms (reversible (competitive, non-competitive, incompetent) and irreversible inhibitors; product inhibition and feed-back inhibition; covalent modifications (binding of phosphoric groups, etc.); proteolytic cleavage; association-dissociation.
Nomenclature and classification of enzymes with examples for each class.
Cofactors and coenzymes: structure and functions of vitamin B3 (niacin) and of vitamin B2 (riboflavin) and of the coenzymes derived [NAD (P), FMN, FAD].
Principles of bioenergetics, synthesis of ATP and its functions
Free energy variation (DG), equilibrium constant, exergonic and endergonic reactions.
Chemical bases of the free energy variation associated with ATP hydrolysis.
ATP functions: coupled reactions and group transfers.
Phosphorylated compounds with high energy content.
Oxidative phosphorylation: respiratory chain and ATP synthase; control, inhibitors and decouplers.
Biochemistry of informational macromolecules
- Nucleotides and nucleic acids: structure and chemical properties of nitrogenous bases, nucleotides and polynucleotide chains; structure and functions of DNA and RNA; gene concept.
- Transcription: structure and properties of eukaryotic RNA polymerases; molecular mechanism of the process; control of transcriptional activity in eukaryotic cells (chemical modifications of histones, chromatin remodeling complexes, DNA methylation, enhancers, silencers, activators and repressors).
- Processing and maturation of pre-mRNAs in eukaryotic cells: mechanism and functions of capping in 5 ', of polyadenylation in 3', of splicing (constitutive and alternative) and of RNA editing.
- Translation: structure and functions of ribosomes and tRNAs, aminoacylation reaction, genetic code, protein synthesis mechanism, folding and post-translational modifications.
- Degradation of mRNA and proteins (lysosomal and ubiquitin-dependent).
- Regulatory RNA: microRNAs.
Prerequisites for admission
The course is for students who have acquired knowledge of inorganic general chemistry and general biology.
Iconographic material of the lessons on the site https://ariel.unimi.it/
- D.L. Nelson, M.M. Cox, "I Principi di Biochimica di Lehninger", Zanichelli, 7°ed., 2018
- N. Siliprandi, G. Tettamanti, "Biochimica Applicata Medica", Piccin, 5°ed., 2018
- T.M.Devlin, "Biochimica con aspetti clinico-farmaceutici", EdiSES, 5° ed., 2013
Assessment methods and Criteria
The exam consists of an oral test which includes a question on each of the following three topics:
- chemical structure of biomolecules;
- classification, kinetics and regulation of enzymes;
- informational macromolecules;
plus further questions on two other topics included in the program.
The exam is considered passed when the student demonstrates knowledge of the required topics.
The criterion for assigning the mark is established on the basis of the level of deepening demonstrated of one's knowledge and on the student's ability to answer questions with appropriate terminology.
In each Academic Year 7 exam sessions will be fixed. These "ordinary" sessions will be scheduled only in the periods in which there is no provision of lessons, namely:
- 1 exam in the autumn suspension period of teaching (usually at the end of November);
- 2 exam sessions between the last week of January and the end of February;
- 1 exam in the spring suspension period of teaching (normally in April)
- 2 exam sessions between mid-June and late July;
- 1 session in September.
In each Academic Year, at the request of the students, two "extraordinary" sessions, reserved for students who are out of course and repeating, can be set even in periods in which there is no suspension of teaching activities.