Biochemistry

A.Y. 2018/2019
9
Max ECTS
80
Overall hours
SSD
BIO/10
Language
Italian
Learning objectives
The course aims to provide a basic knowledge on : (i) structure-to-function relationships among biological (macro)molecules; (ii) energy flux in the cell; (iii) mechanism of action of selected protein classes, with special emphasis on enzymes; (iv) main metabolic pathways, with special reference to their roles, logic of construction and regulation.
Expected learning outcomes
Undefined
Course syllabus and organization

A - L

Responsible
Course syllabus
GOALS
The course aims to provide a basic knowledge on : (i) structure-to-function relationships among biological (macro)molecules; (ii) energy flux in the cell; (iii) mechanism of action of selected protein classes, with special emphasis on enzymes; (iv) main metabolic pathways, with special reference to their roles, logic of construction and regulation.

Edition A-L
Teacher: Martino Bolognesi

PROGRAM
- Bioelements, biomolecules and macromolecules. Water as the biological solvent. Role of weak interactions and pH in macromolecular structure and function.
- Nucleic acids: structure and physico-chemical properties of nucleotides , DNA and RNA.
- Proteins: Structure and properties of amino acids. The peptide bond. Polypeptides.
- Protein structure (primary, secondary, tertiary and quaternary structure; domains and motifs). Solution properties of proteins.
- An introduction to protein purification and structural characterization.
- Protein folding. Achievement of protein 3D structure: the folding process. -
- The basics of the biochemistry of DNA replication and transcription and Protein synthesis.
- Oxygen transport proteins: structure-function relations in myoglobin and hemoglobin.
- Enzymes: principles of enzyme catalysis; cofactors and coenzymes; Stereospecificity and stereochemical control of catalysis.
- Chemical kinetics and enzyme kinetics. Transition state theory. Steady-state kinetics and meaning of kinetic parameters. The Michaelis-Menten equation
- Inhibition and allosteric regulation of enzymes.
- Classification of biological reactions; reaction mechanisms of selected key enzymes.
- Energy changes in biological processes: free energy changes, chemical equilibria, relation between free energy change and oxidoreduction potential. Coupled reactions. Energy flux and high-energy compounds. ATP and metabolic role of phosphate transfer reactions.
- Metabolism: basic aspects of metabolic pathways and methods for their study.
- Glycolysis and fermentations. Gluconeogenesis. Glycogen metabolism and glycogen phosphorylase as an example of an allosterically and covalently regulated enzyme. Pentose phosphate shunt
- The pyruvate dehydrogenase complex.
- The Krebs cycle.
- The oxidative phosphorylation (electron transport chain and ATP synthesis)
- The basics of photosynthesis
- Fatty acid metabolism (beta oxidation and fatty acid biosynthesis)
- Amino acids synthesis and degradation (general principles), urea metabolism.

TUTORIALS
The formal lectures will be complemented by classroom sessions of problem solving, use of animations and molecular graphics and common discussions.

REFERENCE MATERIAL
The use of the latest edition of one of the following basic biochemistry textbooks is highly recommended:
- Appling, Antony-Cahill & Mathews: Biochimica, Molecole e Metabolismo (Pearson 2017)
- Nelson D.L. & Cox M.M. - Lehninger's Principles of Biochemistry, Worth Publishers / Zanichelli (2018)
- Voet D. & Voet, J.G. - Principles of Biochemistry, Wiley & Sons. / Zanichelli (2017)
- Mathews CK, Van Holde KE, Appling DR, Anthony-Cahill DR - Biochemistry- 4th Edition (2013) Pearson


Textbooks, reading material and complementary teaching material
Copies of the slides projected in the classroom as well as other materials will be made available through the course website on the ARIEL platform of the University of Milano (http://ariel.ctu.unimi.it). By no means these materials replace the lectures or a textbook. The material is made available only to registered students of the Degree Course in Biological Sciences and should not be distributed to others.

PREREQUISITES AND EXAMINATION PROCEDURES
The exam will consist of a written test including a combination of open-answer questions and exercises to evaluate the degree of understanding of the topics covered during the lectures.

TEACHING METHODS
Front lectures with power point presentations published in advance in the ARIEL website and use of blackboard as needed. Participation at classes is therefore highly recommended.

LANGUAGE OF INSTRUCTION
Italian with short summaries in English at the end of the lesson.

RECOMMENDED PREREQUISITES
REQUIRED PRELIMINARY KNOWLEDGE
Students must be fully proficient (i.e. they are asked to have passed the respective first year exams) in General and inorganic chemistry and in Organic chemistry; Physical-chemistry; other courses in the first year provide additional useful cultural bases.

PROGRAM INFORMATION
To help participation in the lectures power point slides, and additional material will be published well before the lectures in the ARIEL website

WEB PAGES
http://mbolognesicb.ariel.ctu.unimi.it
BIO/10 - BIOCHEMISTRY - University credits: 9
Practicals: 16 hours
Lessons: 64 hours
Professor: Bolognesi Martino

M - Z

Course syllabus
GOALS
The course aims to provide a basic knowledge on : (i) structure-to-function relationships among biological (macro)molecules; (ii) energy flux in the cell; (iii) mechanism of action of selected protein classes, with special emphasis on enzymes; (iv) main metabolic pathways, with special reference to their roles, logic of construction and regulation.

Edition M-Z
Teacher: Maria Antonietta Vanoni

PROGRAM
- Bioelements, biomolecules and macromolecules. Water as the biological solvent. Role of weak interactions and pH in macromolecular structure and function.
- Nucleic acids: structure and physico-chemical properties of nucleotides , DNA and RNA.
- Proteins: Structure and properties of amino acids. The peptide bond. Polypeptides.
- Protein structure (primary, secondary, tertiary and quaternary structure; domains and motifs). Solution properties of proteins.
- An introduction to protein purification and structural characterization.
- Protein folding. Achievement of protein 3D structure: the folding process. -
- The basics of the biochemistry of DNA replication and transcription and Protein synthesis.
- Oxygen transport proteins: structure-function relations in myoglobin and hemoglobin.
- Enzymes: principles of enzyme catalysis; cofactors and coenzymes; Stereospecificity and stereochemical control of catalysis.
- Chemical kinetics and enzyme kinetics. Transition state theory. Steady-state kinetics and meaning of kinetic parameters. The Michaelis-Menten equation
- Inhibition and allosteric regulation of enzymes.
- Classification of biological reactions; reaction mechanisms of selected key enzymes.

- Energy changes in biological processes: free energy changes, chemical equilibria, relation between free energy change and oxidoreduction potential. Coupled reactions. Energy flux and high-energy compounds. ATP and metabolic role of phosphate transfer reactions.
- Metabolism: basic aspects of metabolic pathways and methods for their study.
- Glycolysis and fermentations. Gluconeogenesis. Glycogen metabolism and glycogen phosphorylase as an example of an allosterically and covalently regulated enzyme. Pentose phosphate shunt
- The pyruvate dehydrogenase complex.
- The Krebs cycle.
- The oxidative phosphorylation (electron transport chain and ATP synthesis)
- The basics of photosynthesis
- Fatty acid metabolism (beta oxidation and fatty acid biosynthesis)
- Amino acids synthesis and degradation (general principles), urea metabolism.

TUTORIALS
The formal lectures will be complemented by classroom sessions of problem solving, use of animations and molecular graphics and common discussions


REFERENCE MATERIAL
The use of the latest edition of one of the following basic biochemistry textbooks is highly recommended:
- Nelson D.L. & Cox M.M. - Lehninger's Principles of Biochemistry, Worth Publishers
- Voet D. & Voet, J.G. - Biochemistry, Wiley & Sons.
- Mathews CK, Van Holde KE, Appling DR, Anthony-Cahill DR - Biochemistry- 4th Edition (2013) Pearson

Textbooks, reading material and complementary teaching material
Copies of the slides projected in the classroom as well as other materials will be made available through the course website on the ARIEL platform of the University of Milano (http://ariel.ctu.unimi.it). By no means these materials substitute for the lectures or a textbook. The material is made available only to registered students of the Degree Course in Biological Sciences and should not be distributed to others.


PREREQUISITES AND EXAMINATION PROCEDURES
The exam will consist of a written test including a combination of open-answer questions and exercises to evaluate the degree of understanding of the topics covered during the lectures.


TEACHING METHODS:
Front lectures with power point presentations published in advance in the ARIEL website and use of blackboard as needed. Participation at classes is therefore highly recommended.


LANGUAGE OF INSTRUCTION
Italian


REQUIRED PRELIMINARY KNOWLEDGE
Students must be fully proficient (i.e. they are asked to have passed the respective first year exams) in General and inorganic chemistry and in Organic chemistry; Physical-chemistry; other courses in the first year provide additional useful cultural bases.


PROGRAM INFORMATION
To favor participation in the lectures power point slides , and additional material will be published well before the lectures in the ARIEL website


WEB PAGES
http://mavanonicb.ariel.ctu.unimi.it
BIO/10 - BIOCHEMISTRY - University credits: 9
Practicals: 16 hours
Lessons: 64 hours
Professor(s)
Reception:
Monday through Friday - previously setting the proper time
Dept. of BioSciences - Building C, 5th floor
Reception:
Monday, 1 pm -2 pm
Protein Biochemistry Unit, DSBB, Via Celoria 26, 5C