Ateneo - UPO

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 and 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. Lipopropeins (Chylomicrons, VLDL, LDL, HDL): structure and function.

Cholesterol homeostasis: fate of cholesterol, role of LDL in cholesterol absorption

HEMOGLOBIN-MYOGLOBIN IRON
Localization and diversity Hemoglobin-Myoglobin. 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.

Titolo CHIMICA e BIOCHIMICA per le lauree triennali (Area Sanitaria)
Autore SAMAJA-PARONI
EDITORE PICCIN

Titolo Elementi di CHIMICA E BIOCHIMICA
Autore ROBERTI, ALUNNI BISTOCCHI
EDITORE McGraw Hill

PER APPROFONDIMENTI:

Titolo LE BASI DELLA BIOCHIMICA
Autore Ferrier
EDITORE Zanichelli
Autore Nelson e Cox

Titolo INTRODUZIONE ALLA BIOCHIMICA DEL LEHNINGER
EDITORE Zanichelli

The student will be able to:
Describe the nutrient structure.
Describe how nutrients are digested and absorbed by the body
Describe how hemoglobin transposes oxygen to cells and which ones
are the factors that regulate this process

The student must have basic notions in: Chemistry
General: chemical bonds, equilibrium and completion reactions;
redox reactions; acids, bases, buffers and solution equilibria
watery. 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 on the structure of the human body

Frontal lessons

Pdf copy of the projected slides, in-depth material and
all information regarding the course and exam methods will be
made available on the DIR (https://www.dir.uniupo.it/ )

The exam will consist of a written test with multiple choice questions, test tests will be available on DIR

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 and 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. Lipopropeins (Chylomicrons, VLDL, LDL, HDL): structure and function.

Cholesterol homeostasis: fate of cholesterol, role of LDL in cholesterol absorption

HEMOGLOBIN-MYOGLOBIN IRON
Localization and diversity Hemoglobin-Myoglobin. 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.

the student will be able to:
Describe the nutrient structure.
Describe how nutrients are digested and absorbed by the body
Describe how hemoglobin transposes oxygen to cells and which ones
are the factors that regulate this process