General Biochemistry
A.Y. 2023/2024
Learning objectives
The course provides the required terminology and fundamental principles for the study of the metabolic processes that will be developed in the course of the third year Metabolic and Functional Biochemistry. In particular, the aim of the course of General Biochemistry is to lead the student through a path that allows him to acquire the knowledge related to:
- structure, chemical-physical properties, and functions of the main "simple" organic biomolecules (amino acids, carbohydrates, lipids, and nucleotides) of specific relevance for the human being;
- chemical-physical bases that promote the assembly of these "simple" organic biomolecules to form macromolecules and functional supramolecular complexes (proteins, polysaccharides, nucleic acids, biological membranes) so as to understand the structure-function relationship;
- bioenergetics in the human being: mechanisms for energy extraction, conservation and utilization;
- kinetics of chemical reactions, functions and regulation of enzymes.
The course also provides for the basic principles related to the biochemistry of informational macromolecules (DNA, RNA and proteins) with notions concerning their structure, properties, metabolism and cellular functions.
- structure, chemical-physical properties, and functions of the main "simple" organic biomolecules (amino acids, carbohydrates, lipids, and nucleotides) of specific relevance for the human being;
- chemical-physical bases that promote the assembly of these "simple" organic biomolecules to form macromolecules and functional supramolecular complexes (proteins, polysaccharides, nucleic acids, biological membranes) so as to understand the structure-function relationship;
- bioenergetics in the human being: mechanisms for energy extraction, conservation and utilization;
- kinetics of chemical reactions, functions and regulation of enzymes.
The course also provides for the basic principles related to the biochemistry of informational macromolecules (DNA, RNA and proteins) with notions concerning their structure, properties, metabolism and cellular functions.
Expected learning outcomes
At the end of the course of General Biochemistry, the student will have acquired the terminology and will have the knowledge of the structure, chemical-physical properties, and functions of the main organic biomolecules of specific relevance for the human being. The student will have also learned the principles of the thermodynamic and kinetic control of the chemical reactions occurring in human cells, and the basic principles of the transmission of information contained in the genome.
Lesson period: Second semester
Assessment methods: Esame
Assessment result: voto verbalizzato in trentesimi
Single course
This course cannot be attended as a single course. Please check our list of single courses to find the ones available for enrolment.
Course syllabus and organization
Linea AL
Responsible
Lesson period
Second semester
Course syllabus
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
Amino Acids
-Structure, properties and classification. Peptide bond.
Proteins
-Structure and function.
-Globular Proteins: Myoglobin; Haemoglobin; Albumin; Globulins.
-Fibrous Proteins: Collagen; Elastin; Keratins;
-Glycoproteins and Proteoglycans.
Carbohydrates
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, chitin and other vegetal polysaccharida;
- heteropolysaccharides: glycosaminoglycans (main classes) and proteoglycans.
Lipids
Structure and functions of:
- saturated and unsaturated fatty acids: nomenclature and numbering);
- triglycerides, glycerolphospholipids, sphingolfospholipids, glycosphingolipids and cholesterol;
- lipid aggregates: micelles, liposomes.
Membranes
-Fluid mosaic model.
-Transport mechanisms (simple and facilitated diffusions; active transport; channel proteins; Na+,K+-ATPase and Ca++ATPase pumps).
BASES, NUCLESIDES AND NUCLETIDES
Structure, chemical properties and functions of nucleotides and polinucleotide chains (DNA and RNA)
Causes and consequences of chemical modifications (spontaneous or induced) of nucleotides.
Thermodynamic principles
-Change of free energy in standard conditions.
-Phosphate and thioester compounds with high-energy bonds.
-ATP hydrolysis and coupling of exoergonic and endoergonic processes.
Enzymes
Properties and structural features, constitutive and inducible enzymes.
Enzymatic kinetics: Michaelis-Menten, Vmax and Km equation; graph of reciprocal doubles.
Influence of pH and temperature; inhibition mechanisms (reversible (competitive, non-competitive, incompetent) and irreversible inhibitors;
Regulation of enzyme activity: product inhibition; Covalent modifications (binding of phosphoric groups, etc., Allosteric enzymes and feed-back inhibition; association-dissociation; proteolytic cleavage; isoenzymes, and inducible enzymes
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].
Bioenergetics
-Mitochondria.
-Respiratory chain (components and sequential processing; control mechanisms; inhibitors and uncouplers).
-Oxidative phosphorylation.
-Mitochondrial carriers.
Water, acids and bases, pH and buffer systems in the human body
Amino Acids
-Structure, properties and classification. Peptide bond.
Proteins
-Structure and function.
-Globular Proteins: Myoglobin; Haemoglobin; Albumin; Globulins.
-Fibrous Proteins: Collagen; Elastin; Keratins;
-Glycoproteins and Proteoglycans.
Carbohydrates
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, chitin and other vegetal polysaccharida;
- heteropolysaccharides: glycosaminoglycans (main classes) and proteoglycans.
Lipids
Structure and functions of:
- saturated and unsaturated fatty acids: nomenclature and numbering);
- triglycerides, glycerolphospholipids, sphingolfospholipids, glycosphingolipids and cholesterol;
- lipid aggregates: micelles, liposomes.
Membranes
-Fluid mosaic model.
-Transport mechanisms (simple and facilitated diffusions; active transport; channel proteins; Na+,K+-ATPase and Ca++ATPase pumps).
BASES, NUCLESIDES AND NUCLETIDES
Structure, chemical properties and functions of nucleotides and polinucleotide chains (DNA and RNA)
Causes and consequences of chemical modifications (spontaneous or induced) of nucleotides.
Thermodynamic principles
-Change of free energy in standard conditions.
-Phosphate and thioester compounds with high-energy bonds.
-ATP hydrolysis and coupling of exoergonic and endoergonic processes.
Enzymes
Properties and structural features, constitutive and inducible enzymes.
Enzymatic kinetics: Michaelis-Menten, Vmax and Km equation; graph of reciprocal doubles.
Influence of pH and temperature; inhibition mechanisms (reversible (competitive, non-competitive, incompetent) and irreversible inhibitors;
Regulation of enzyme activity: product inhibition; Covalent modifications (binding of phosphoric groups, etc., Allosteric enzymes and feed-back inhibition; association-dissociation; proteolytic cleavage; isoenzymes, and inducible enzymes
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].
Bioenergetics
-Mitochondria.
-Respiratory chain (components and sequential processing; control mechanisms; inhibitors and uncouplers).
-Oxidative phosphorylation.
-Mitochondrial carriers.
Prerequisites for admission
The course is for students who have acquired knowledge of inorganic general chemistry and general biology.
Teaching methods
Frontal lectures (6 credits)
Teaching Resources
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, 8°ed., 2022
- N. Siliprandi, G. Tettamanti, "Biochimica Applicata Medica", Piccin, 5°ed., 2018
- D.L. Nelson, M.M. Cox, "I Principi di Biochimica di Lehninger", Zanichelli, 8°ed., 2022
- N. Siliprandi, G. Tettamanti, "Biochimica Applicata Medica", Piccin, 5°ed., 2018
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.
- 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.
Linea MZ
Responsible
Lesson period
Second semester
Course syllabus
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
Amino Acids
Structure, classification, chemical properties and functions. Peptide bond.
Proteins
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.
Carbohydrates
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.
Nucleotides
Structure, chemical properties and functions of nucleotides and polinucleotide chains (DNA and RNA)
Causes and consequences of chemical modifications (spontaneous or induced) of nucleotides.
Lipids
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.
Biological membranes
Composition, structure and properties (asymmetry, fluidity and dynamism).
Membrane proteins: structure and functions.
Transport mechanisms: simple and facilitated diffusion, active transport, channel proteins, ionophores.
Enzymes
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.
Allosteric enzymes.
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.
Water, acids and bases, pH and buffer systems in the human body
Amino Acids
Structure, classification, chemical properties and functions. Peptide bond.
Proteins
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.
Carbohydrates
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.
Nucleotides
Structure, chemical properties and functions of nucleotides and polinucleotide chains (DNA and RNA)
Causes and consequences of chemical modifications (spontaneous or induced) of nucleotides.
Lipids
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.
Biological membranes
Composition, structure and properties (asymmetry, fluidity and dynamism).
Membrane proteins: structure and functions.
Transport mechanisms: simple and facilitated diffusion, active transport, channel proteins, ionophores.
Enzymes
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.
Allosteric enzymes.
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.
Prerequisites for admission
The course is for students who have acquired knowledge of inorganic general chemistry and general biology.
Teaching methods
Lectures (6 credits)
Teaching Resources
Iconographic material of the lessons on the site https://ariel.unimi.it/
- N. Siliprandi, G. Tettamanti, "Biochimica Applicata Medica", Piccin, 5°ed., 2018
- D.L. Nelson, M.M. Cox, "I Principi di Biochimica di Lehninger", Zanichelli, 7°ed., 2018
- T.M.Devlin, "Biochimica con aspetti clinico-farmaceutici", EdiSES, 2013
- N. Siliprandi, G. Tettamanti, "Biochimica Applicata Medica", Piccin, 5°ed., 2018
- D.L. Nelson, M.M. Cox, "I Principi di Biochimica di Lehninger", Zanichelli, 7°ed., 2018
- T.M.Devlin, "Biochimica con aspetti clinico-farmaceutici", EdiSES, 2013
Assessment methods and Criteria
The exam consists of an oral test which includes a question on each of the following two topics:
- chemical structure and properties, and function of biomolecules;
- classification, kinetics and regulation of enzymes;
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 (1 extraordinary "spring session" session in March or May; 1 extraordinary "autumn session" session in October or December).
- chemical structure and properties, and function of biomolecules;
- classification, kinetics and regulation of enzymes;
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 (1 extraordinary "spring session" session in March or May; 1 extraordinary "autumn session" session in October or December).
Educational website(s)
Professor(s)