Module Details

Structural biochemistry

MS0836

Course
Structural biochemistry
Code
MS0836
Academic Year
2026/2027
Curriculum Year
2026/2027
Degree Programme
NURSING
Curriculum
000 - CORSO GENERICO
Course coordinator
Lecturers
Credits
1
Lecture Hours
12
Scientific Disciplinary Sector (SSD)
BIOS-07/A - Biochemistry
Course Type
Single-subject learning activity
Course Delivery
OBB - Obbligatoria
Year
1
Teaching period
Primo Semestre
Campus
ALBA
Teaching language
Italian
Course Contents
Proteins: structure; Dietary protein digestion: role and nature of zymogens. Amino acids: classification; definition of essential and non-essential. Carbohydrates: Structure: Monosaccharides, definition of epimers and isomers of glucose; Disaccharides: glycosidic bond; Polysaccharides: structure of glycogen, starch and cellulose. Digestion of sugars; lactase deficiency. Structure of glycosaminoglycans, proteoglycans and glycoproteins. Lipids: Structure of triacylglycerols, phospholipids, saturated and unsaturated fatty acids, essential fatty acids. Digestion and absorption of food lipids: role of bile salts and pancreatic lipases. Lipoproteins (Chylomicrons, VLDL, LDL, HDL): structure and function. Cholesterol homeostasis: fate of cholesterol, role of LDL in cholesterol absorption. Hemoglobin-myoglobin: localization and diversity. Functions of hemoglobin: O2 and CO2 transport, heme. Comparisons of hemoglobin: T and R. Cooperativity of O2 binding. O2 dissociation curve. Regulating the affinity of hemoglobin for O2: Bohr effect; Role of the 2,3BPG. Carbon monoxide: binding to hemoglobin and influence on O2 saturation. Types of hemoglobin: HbA, HbA2, HbA1c, HbF, HbS, met-Hb. ENZYMES: What is an enzyme; role of ions and coenzymes; vitamins. Classification of enzymes. Properties of enzymes. How enzymes work: definition of active site, catalysis mechanisms. Regulation of enzymatic activity: substrate concentration (Km and Vmax), temperature, pH, inhibitors/activators, covalent modification, allosteric enzymes.
Reference Texts
Title: Chemistry and Biochemistry for Bachelor's Degree Programs (Health Sciences)
Authors: Samaja, Paroni
Publisher: Piccin
Title: Elements of Chemistry and Biochemistry
Authors: Roberti, Alunni Bistocchi
Publisher: McGraw-Hill
For further reading:
Title: Lippincott Illustrated Reviews: Biochemistry (Italian edition: Le basi della Biochimica)
Author: Ferrier
Publisher: Zanichelli
Title: Lehninger Principles of Biochemistry (Italian edition: Introduzione alla Biochimica di Lehninger)
Authors: Nelson, Cox
Publisher: Zanichelli
Learning Outcomes
Upon successful completion of the course, students will be able to:
-describe the structure and function of the major biomolecules (proteins, carbohydrates, and lipids);
-explain the digestion, absorption, and transport of nutrients, as well as the main mechanisms of cholesterol homeostasis;
-describe the structure and function of hemoglobin and myoglobin, including the mechanisms regulating oxygen transport;
-explain the structure, function, classification, and regulation of enzymes, including the basic principles of enzyme kinetics;
-apply fundamental biochemical knowledge to the interpretation of major physiological processes and clinically relevant conditions.
Prerequisites
The student must have basic notions in:
General Chemistry: chemical bonds, equilibrium and completion reactions; redox reactions; acids, bases, buffers and aqueous solution equilibria.
Organic Chemistry: functional groups, alkenes, alcohols, thiols, aromatic compounds, aldehydes, ketones, carboxylic acids and their derivatives. Main chemical and physical characteristics of the above compounds. Stereochemistry.
Physics: the laws of thermodynamics, in particular Gibbs free energy.
Biology: structure of the eukaryotic cell
Anatomy: basic knowledge of the structure of the human body
Teaching Methods
The course is delivered through face-to-face lectures and, where applicable, online lectures, supported by teaching materials made available through the University's online learning platform.
Additional Information
PDF copies of the lecture slides, supplementary learning materials, and all information concerning the course and examination procedures will be made available on the DIR platform (https://www.dir.uniupo.it/).
Students with disabilities, Specific Learning Disorders (SLD), or Special Educational Needs (SEN) may request specific services and support tools dedicated to them by contacting the University’s Student Careers Development and Coordination Staff and Student Services Office, and by consulting the dedicated page on the University website: https://uniupo.it/it/servizi/servizi-studentesse-e-studenti-condizione-di-disabilit%C3%A0-e-dsa.
Students with disabilities, SLD, or SEN, once they have contacted the University’s relevant staff, may contact the course instructor regarding the arrangements for examination procedures and any aspects related to teaching and learning activities.
Assessment Methods
The exam will consist of a written test with multiple choice questions, test tests will be available on DIR
Detailed Syllabus
Proteins and amino acids
Structure and function of proteins. Digestion of dietary proteins: role and nature of zymogens. Amino acid classification and definition of essential and non-essential amino acids.
Carbohydrates
Structure of monosaccharides; glucose epimers and isomers. Disaccharides and glycosidic bonds. Polysaccharides: structure and function of glycogen, starch, and cellulose. Carbohydrate digestion and lactase deficiency. Structure and function of glycosaminoglycans, proteoglycans, and glycoproteins.
Lipids
Structure of triacylglycerols, phospholipids, and saturated, unsaturated, and essential fatty acids. Digestion and absorption of dietary lipids: role of bile salts and pancreatic lipases. Plasma lipoproteins (chylomicrons, VLDL, LDL, HDL): structure and function. Cholesterol homeostasis and the role of LDL in cholesterol transport and uptake.
Hemoglobin, myoglobin, and iron metabolism
Localization and structural features of hemoglobin and myoglobin. Hemoglobin functions in oxygen and carbon dioxide transport. Heme structure. T and R conformations of hemoglobin, cooperative oxygen binding, and oxygen dissociation curve. Regulation of oxygen affinity: Bohr effect and role of 2,3-bisphosphoglycerate. Carbon monoxide interaction with hemoglobin. Main hemoglobin forms: HbA, HbA₂, HbA1c, HbF, HbS, and methemoglobin.
Enzymes
Definition and properties of enzymes. Role of ions, coenzymes, and vitamins. Enzyme classification and characteristics. Active site and mechanisms of enzymatic catalysis. Regulation of enzyme activity: substrate concentration, kinetic parameters Km and Vmax, temperature, pH, inhibitors and activators, covalent modifications, and allosteric enzymes.
Expected Learning Outcomes
At the end of the course, the student will be able to:
-describe the structure and main chemical characteristics of nutrients;
-explain the processes of digestion and absorption of nutrients in the body;
-describe the role of hemoglobin in oxygen transport to tissues and the main factors regulating its oxygen affinity.
Last update:09-09-2026 00:14:31