Unit BIOCHEMISTRY
- Course
- Biological sciences
- Study-unit Code
- 55008608
- Curriculum
- In all curricula
- Teacher
- Lorena Urbanelli
- Teachers
-
- Lorena Urbanelli
- Hours
- 56 ore - Lorena Urbanelli
- CFU
- 8
- Course Regulation
- Coorte 2022
- Offered
- 2023/24
- Learning activities
- Caratterizzante
- Area
- Discipline biomolecolari
- Academic discipline
- BIO/10
- Type of study-unit
- Obbligatorio (Required)
- Type of learning activities
- Attività formativa monodisciplinare
- Language of instruction
- Italian
- Contents
- The aim of the course is to illustrate students the structure/activity relation of the main classes of biological macromolecules (protein, carbohydrates, lipids), with a focus on the structure/activity relation of proteins as enzymes and transporters. Further, the course will introduce cellular energy metabolism and will outline the main catabolic routes for the energetic use of carbohydrates, lipids and amino acids
- Reference texts
- Nelson, M.M.Cox, Lehninger Principles of Biochemistry, Ed. Macmillan
- Educational objectives
- Students will acquire knowledge on the structure/function relation of the main classes of biological macromolecules (protein, carbohydrates, lipids), and in detail on the structure/function relation of proteins, with a focus on specific examples, such as enzymes and transport proteins. Further, students will acquire knowledge on cell energy metabolism and on the main features of energy macromolecule catabolism (carbohydrates, lipids, aminoacids). A central goal is understanding the main structural and functional features of the cell chemical constituents of the living matter and the main characteristics allowing the energetic use of biological constituents.
- Prerequisites
- A prerequisite of the course are basic notions of General Biology (eukaryotic and prokaryotic cell organization), of General Chemistry (chemical bonds, pH and solutions, redox reactions) and of on Organic Chemistry (properties of the main functional groups of the carbon chemistry).
- Teaching methods
- The course is based on i) lessons with slides, ii) video on specific lesson topics, iii) test with multiple choice and open questions on course topics, iv) simulation of the written test.
- Other information
- For the teaching calendar (lessons date, time and place), please check the Biological Sciences degree website in dcbb.unipg.it
- Learning verification modality
- The final examination will consist in a written test on all topics (40 min, 30 multiple choice questions) to assess the basic comprehension of the course topics and an oral examination for students with a sufficient evaluation in it (18/30), in order to discuss the critical points emerged.
Students that will not reach a sufficient evaluation in the written part (18/30) may discuss the critical points during the oral examination or with the teacher by appointment
Should exam face-to-face not allowed, final examination will be carried out via an online platform in agreement with the University regulation
Students with disabilities or DSA may consult the webpage www.unipg.it/disabilita-e-dsa - Extended program
- Characteristics and classification of amino acids. Acid-base properties. Modified amino acids and amino acid derivatives. The peptide bond. Peptide isoelectric point. Protein structural levels (primary, secondary, tertiary and quaternary). Protein secondary structure: alpha-helices, beta sheets, beta folding. Tertiary structure and weak interactions: hydrogen bonds, electrostatic interactions, hydrophobic interactions and van der Waals forces. Protein folding and denaturation. Fibrous proteins: keratin, collagen, fibroin. Myoglobin: structure, heme group, oxygen binding curve. Hemoglobin: oxygen binding curve, T-R state transition. Bohr effect and CO2 transport.
The enzymes. Kinetics and reaction coordinate of catalyzed and uncatalyzed reactions. The transition state. Enzyme-substrate interaction. Michaelis and Menten kinetics: concept of initial velocity and steady state. The linearization of the Michaelis-Menten equation. Reversible and irreversible inhibitors. Reversible inhibitors: kinetic aspects. Regulation of enzyme activity: reversible and irreversible mechanisms. Lipids: chemical-physical characteristics. Fatty acids: length, saturation, and nomenclature. Triglycerides and phosphoglycerides. The sphingolipids. Cholesterol: characteristics and role in biological membranes. Carbohydrates: aldose and ketoses monosaccharides. The epimers. The cyclization. Disaccharides: the glycosidic bond. Polysaccharides: reserve and structural functions.
Metabolism: endergonic and exergonic reactions. Coupled reactions: the role and structure of ATP. Coenzyme A, pyridine coenzymes, flavin coenzymes. Glycolysis: investment phase and energy recovery phase. Lactic and alcoholic fermentation. Gluconeogenesis: the different stages with respect to glycolysis. The pentose phosphate pathway: oxidative phase and non-oxidative phase. The pyruvate dehydrogenase. The Krebs cycle. Anaplerotic reactions. The electron transport chain. The formation of the chemiosmotic gradient. ATP synthase: F0 and F1 subunits. The rotational catalysis of ATP. The beta-oxidation of fatty acids. Ketone bodies. The urea cycle: the synthesis of carbamyl phosphate. The mitochondrial phase and the cytosolic phase.