OVERVIEW

 The course of Biological Chemistry aims to provide students with the basic biochemical knowledge for the acquisition of theoretical-practical skills fundamental for the study that will be addressed, at the molecular and systemic level, following the teachings of the Bachelor of Science Degree as well as of any Master's degree courses.

AIMS AND CONTENT

LEARNING OUTCOMES

At the end of the lessons and laboratories of the "Biological Chemistry and laboratory" classes, the student will know: - biological processes at the molecular level; - structure-function relationships of biomolecules; - energy metabolism; - an integrated view of the signal - the main metabolisms - the basics of structural biochemistry and enzymology.

AIMS AND LEARNING OUTCOMES

Attendance and participation in the planned educational activities (frontal lessons and laboratory experiences) will allow the student to acquire the necessary knowledge to face the study of Physiology, Pathology, Molecular Biology and Advanced Biochemistry.

Specifically, the student will be able to understand, learn and describe, at a molecular level, the structure-function relationship of metabolites and proteins with particular attention to those with enzyme activity. He will be able to use this knowledge for the learning of biochemistry of the main catabolic and anabolic processes.

PREREQUISITES

Fundamental requirements for the study of biochemistry are the knowledge of general, inorganic and organic chemistry.
In particular the student will have to know in detail: chemical kinetics, buffer systems, chemical equilibria, functional groups of biological interest and their main reactions.

TEACHING METHODS

The teaching consists of lectures and laboratory activities. Activities aimed at applying the knowledge acquired in the classroom during the lectures are foreseen. Also for this reason attendance at lectures and laboratory exercises is strongly recommended.

Lectures in the classroom are delivered through the use of multimedia presentations and the constant use of the blackboard for the writing of molecular structures and the description of the different metabolic pathways.

The laboratory exercises include the drawing up of individual reports which will be discussed with the teacher during the examination phase.

The laboratory exercises take place in equipped laboratories present at the DISTAV - second floor of the Palazzo delle Scienze and in the CEBR laboratories.

Due to the evolution in the health and epidemiological situation, please refer to the specific AulaWeb  course page  for any updates 

SYLLABUS/CONTENT

Biomolecules and their structure

Carbohydrates

Functional groups of organic compounds of biochemical interest. Definition, raw and structure formula of carbohydrates. Identification of chiral and sugar stereochemical centers. Furanosic and piranosic forms. Structure and formation of hemiacetal bonds in the hexoses and pentoses, with the formation of new centers of asymmetry: alfa and beta anomers. Sugar structures: glucose, galactose, mannose and fructose, ribose and deoxyribose. Glycosidic bonds; structure disaccharides, sucrose and lactose. Polysaccharides structure of biochemical interest. Reducing and non-reducing ends of polysaccharides. Cellulose structure.

Nitrogenous Bases and Nucleic Acids

Pyrimidine and Purinie bases and their tautomeric forms. Nucleosides and nucleotides, structure of ATP, ADP and AMP. Deoxy nucleosides and nucleotides. Esters and pyrophosphoric bonds of ATP. Phosphodiester bond.

Amino Acids and Proteins

General Properties of Standard aminoacids (AA). Chirality of Amino Acids Distribution in  classes of 20 Standard Amino Acids. Definition of Amino Acid Standard and its correlations with the Genetic Code. Formation of the peptide bond and its geometric isomerism. Definition of polypeptide and protein. Primary structure of a protein. N- and C-terminal amino acids of a polypeptide and/or protein. Definition of phi and psi twist angles. Ramachandran Plot. Regular protein folding formulas and details about the formation of hydrogen bonds: parallel and anti-parallel folded sheets. Major regular structures of proteins. Myoglobin and hemoglobin and their structure. Bohr effect.

Coenzymes and Vitamins

Vitamins and Coenzymes. NAD+ and NADP+ pyridine co-enzymes: oxide/reductive interconversions with hydrogen ion transfer mechanism.

Metabolism

Generality, convergence and divergence of the metabolic pathways. Regulation. Energy metabolism and regulatory metabolism. Glutathione metabolism.

Glycolysis.Glycogen.Gluconeogenesis. Pyruvic acid oxidative decarboxylation. Krebs cycle with mass balance and energy balance. Cory Cycle. Anaplerotic reactions. Electron transport chain. Respiratory Compounds. Uncoupling. Oxygen reactive derivatives. Shuttle systems. ADP-ATP translocase. Lipid metabolism. Lipase. Carnitine. B -oxidation of saturated and monounsaturated chains fatty acids. Ketone bodies. Saturated fatty acid biosynthesis. Triglycerides and phospholipids biosynthesis. Nitrogen metabolism. Carbamyl Phosphate Synthesis. Transaminase (GPT and GOT). Deamination of glutamate. Ammonia toxicity. Glutamine synthetase. Alanine cycle. Urea cycle..

Biochemical Methods (Laboratory) :. Spectrophotometry. Absorption spectra and use of pyridine coenzyme. Proteins assays in cell specimens by spectrophotometric methods. Determination of enzymatic activity in raw organic preparations: Glucose 6 Phosphate Dehydrogenase. Determination of kinetic parameters of the G6PD enzyme. Principles of gas chromatography and its application for qualitative and quantitative analysis of fatty acids. Qualitative and Quantitative Determination of Adenyl Nucleotides by High Performance Liquid Chromatography. Protein sequencing by mass spectrometry; Protein digestion.

RECOMMENDED READING/BIBLIOGRAPHY

All slides used during the lessons and other educational material will be available on AulaWeb at the end of each cycle of lectures / laboratory exercises along with other bibliographic material in pdf format.

The books indicated are suggested as a supporting text and are available and can be consulted together with other books for further information by the teacher.

Texts advised for further information:Voet-Voet-Pratt Fondamenti di Biochimica-Zanichelli
Nelson-Cox-I principi di biochimica di Lehninger -Zanichelli
Berg-Tymoczko-Stryer-Biochimica - Zanichelli
Garret-Grisham – Principi di Biochimica- Piccin
Ringe-Petsko- Struttura e funzione delle proteine- Zanichelli

TEACHERS AND EXAM BOARD

Exam Board

GIANLUCA DAMONTE (President)

MIRKO BENVENUTI

ENRICO MILLO (President Substitute)

ANNALISA SALIS (President Substitute)

FRANCESCO PIACENTE (Substitute)

LESSONS

LESSONS START

For lessons start and timetable go to the link: https://easyacademy.unige.it/portalestudenti/

Please check the module Aulaweb page for timetable updates dependent on the sanitary and epidemic situation.

Class schedule

BIOLOGICAL CHEMISTRY AND LABORATORY

EXAMS

EXAM DESCRIPTION

The oral exam lasts about 30 minutes / student on the topics covered in class and in practice.
Usually the student is asked three questions of increasing difficulty aimed at assessing the degree of deepening of the subject and preparation of the student.

ASSESSMENT METHODS

Details on how to prepare for the exam and the degree of detail required for each topic will be provided at the beginning of the course and confirmed during lectures and exercises.

The laboratory reports will be delivered online on AulaWeb and will be discussed during the examination.

The oral exam will mainly focus on the topics covered during the lectures and will aim to assess the achievement of the appropriate level of knowledge, the ability to use theoretical notions to integrate the different key concepts of metabolism and the key role of some molecules. The ability to present the topics clearly and with correct terminology will also evaluated.

Due to the evolution in the health and epidemiological situation, please refer to the specific AulaWeb  course page  for any updates 

Exam schedule

FURTHER INFORMATION

Attendance at lectures is strongly recommended.
Attendance at laboratory activities is mandatory