OVERVIEW

The course of Biomedical Chemistry aims to provide the student with the basic biochemical knowledge for the acquisition of fundamental theoretical and practical skills to follow the Graduate Degree Courses in Biological Sciences

AIMS AND CONTENT

LEARNING OUTCOMES

At the end of the course, the student should knows: - biological processes at the molecular level; - biomolecular structure-function relationships; - energy metabolism; - the main metabolic processes; - the basics of biochemistry and enzymology.

AIMS AND LEARNING OUTCOMES

Acquisition of basic knowledge on the structure and function of proteins with particular attention to those with enzymatic activity. To use this  knowledge for the molecular, biochemical understanding of the main catabolic and anabolic processes.

TEACHING METHODS

Frontal lessons. Laboratory exercises

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

Principles of Biochemistry - Garrett, Grisham - : Piccin

Fundamentals of Biochemistry - Voet, Voet, Pratt - : Zanichelli

Biochemistry - Campbell, Farrell - : EdiSES

Principles of Biochemistry Lehninger - Nelson, Cox - : Zanichelli

Biochemistry - Stryer, Timoczcko, Berg - : Zanichelli

TEACHERS AND EXAM BOARD

Exam Board

GIANLUCA DAMONTE (President)

ENRICO MILLO

ANNALISA SALIS

LESSONS

LESSONS START

 February 21st, 2018

Class schedule

BIOLOGICAL CHEMISTRY AND LABORATORY

EXAMS

EXAM DESCRIPTION

Oral exam (about 30-40 minutes / student) on the topics covered in class and exercise.
Usually the student is asked three questions of increasing difficulty aimed at assessing the degree and depth of the student's preparation.

ASSESSMENT METHODS

Knowledge assessment of: protein structure, enzymology, binding and transporting oxygen proteins, glucidic, lipidic and proteic metabolism, molecular structure formulas involved in catabolic and anabolic processes.

Exam schedule