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 other biological courses within the Degree in Chemistry

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

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, fructose, ribose. Glycosidic bonds. Polysaccharides structure of biochemical interest (glycogen). Reducing and non-reducing ends of polysaccharides.

Nucleosides and nucleotides, structure of ATP, ADP and AMP. 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. 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. 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. Cory Cycle. Electron transport chain. Respiratory Compounds. Uncoupling. Oxygen reactive derivatives. ADP-ATP translocase. Lipid metabolism. Lipase. Carnitine. B -oxidation of saturated fatty acids. Ketone bodies. Saturated fatty acid biosynthesis. Nitrogen metabolism. Carbamyl Phosphate Synthesis. Deamination of glutamate. Ammonia toxicity. Glutamine synthetase. Alanine cycle. Urea cycle.

RECOMMENDED READING/BIBLIOGRAPHY

Principles of Biochemistry - Garrett, Grisham - : Piccin

Principles of Biochemistry Lehninger - Nelson, Cox - : Zanichelli

Biochemistry - Stryer, Timoczcko, Berg - : Zanichelli

Didactic material on AulaWeb

TEACHERS AND EXAM BOARD

Exam Board

UMBERTO BENATTI (President)

GIANLUCA DAMONTE (President)

LESSONS

LESSONS START

16 october 2017

Class schedule

The timetable for this course is available here: Portale EasyAcademy

EXAMS

EXAM DESCRIPTION

Oral exam 

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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

FURTHER INFORMATION

The presence at lessons is strongly recommended