Ateneo - UPO

Chemical bonds and interactions between molecules in the chemistry of
life. Structure, classification and function of biological macromolecules.
Simple and complex glycides; lipids and structure of biological
membranes. Nucleic acids and general mechanisms of information
transmission. Amino acids and proteins: structures and folding. Co and
post-translational modifications of proteins and signals for localization.
Cellular addressing processes.
Enzymes and enzymatic kinetics- Extracellular transport proteins,
proteins that bind oxygen, iron and copper.
Contractile structural unit: morphological and molecular organization of
muscle fiber, myofibrils and sarcomere.
Proteins of the cytoskeleton
Protein of the extracellular matrix: laminins, fibronectin, collagens,
elastin.
Transport of molecules: biochemistry of vesicular traffic - Transport of
molecules through the membranes: transporters and channels.
Transmission of regulatory signals from outside into the cell: fundamental
mechanisms of signal transduction. The main signaling pathways in
multicellular organisms

Donald Voet, Judith G Voet, Charlotte W Pratt. PRINCIPI DI BIOCHIMICA,
2017. Zanichelli.
Introduzione allo studio delle proteine. Duranti; Zanichelli
Donald Voet, Judith G Voet, Charlotte W Pratt. FONDAMENTI DI
BIOCHIMICA. IV edizione, 2017. Zanichelli
David L Nelson, Michael M Cox. PRINCIPI DI BIOCHIMICA DI LEHNINGER.
VII edizione, 2018. Zanichelli
Umberto Mura. ENZIMI IN AZIONE. EdiSES, 2012

To provide students with the fundamentals of a molecular approach to physiology and pathology by defining the structure-function relationship of biological macromolecules, with particular emphasis on enzymes, transport proteins, and proteins involved in signal transduction. By the end of the course, students will be able to describe the structure of biological matter in molecular terms and recognize the role of structure in the function of these macromolecules. Furthermore, they must demonstrate a command of the principal mechanisms of enzyme action and the types of reactions catalyzed by enzymes, as well as acquire an adequate understanding of signal transduction mechanisms.

Basic knowledge of general chemistry, organic chemistry, physics and
cell biology

Frontal lesson with the projection of slides, and movies. Execution of
problems and quizzes in the classroom. Ability to run problems and
quizzes at home via the moodle platform. Students can also use the
recommended textbooks to deepen the topics discussed in the classroom

A pdf copy of the projected slides, the in-depth material and all the
information regarding the course and the exam procedures will be made
available on the DIR.
The teacher is available, by appointment, to provide clarification on
specific topics even outside of class time.
Students with disabilities, DSA, BES, once they have contacted the University Staff, can contact the teacher in charge of the course in relation to the declination of the exam methods, regarding the teaching aspects.

In itinere test will be carried out during th course. These tests will NOT be
used for evaluation purposes, but will allow the student to assess his
preparation level regarding the different topics. The objective of the
exam consists in verifying the level of knowledge of the topics of the
course program and the reasoning skills developed by the student. The
exam consists in a written exam consisting of 50 questions related to all
the topics of the course program divided into: quizzes with multiple
choice answers, true / false response, recognition of molecular structures,
numerical problems. Sufficiency is reached by answering correctly to
27/50 questions. The evaluation is expressed in thirtieths (minimum mark
18). During the written test it is not allowed to consult any kind of
material. The calculator is allowed. The exam allows to evaluate the
knowledge (theoretical questions), the skills and the ability to apply the
knowledge learned (exercises), the critical sense, the ability to
understand the text and the ability to apply the knowledge learned
(exercises with request to operate a choice between different
alternatives)

1_ The biological macromolecules. The chemical bonds and the
interactions between molecules in the chemistry of life. Carbohydrates.
Monosaccharides, disaccharides, glycosidic bond. Omopolysaccharides,
modified monosaccharides, heteropolisaccharides: glycosaminoglycans,
chitin, agar, hemicellulose, gums. Glycoconjugates: glipicans, sindecans,
proteoglycans, glycoproteins. Lipids. Saturated and unsaturated fatty
acids. Neutral glycerides and waxes, glycerophospholipids, plasmalogens,
sphingolipids, glycolipids. Principles of organization of biological
membranes. Cholesterol structure and its derivatives. Nucleic acids.
Nitrogenous bases, nucleosides, nucleotides. The phosphodiester bond,
primary and secondary structure of nucleic acids. DNA denaturation and
duplication of information. Amino acids: structure, stereoisomerism and
chirality. Reversible modifications of amino acids involved in protein
regulation. Isoelectric point. Proteins. Peptide bond: chemical and
physical properties. Outline of the derived molecules of amino acids with
biological activity. The directionality of the amino acid sequence; hints on
the conversion of the genetic code into an amino acid sequence
(translation of mRNA). Secondary structures, tertiary structure. Bridge
disulfide bonds. Supersecondary structures, structural motifs and
functional domains. Tertiary structure. Folding. Quaternary structure:
fibrous proteins and globular proteins. Immunoenzymatic methods for the
study of protein structure: immunoblot / Western Blot, Enzyme Linked
Immuno Sorbent Assay (ELISA)
2_Enzymes and enzymatic kinetics. The laws of thermodynamics in
biological reactions. Activation energy its impact on the reaction speed.
Speed constant. Enzymes, coenzymes, prosthetic groups, co-substrates:
general mechanisms of action. Classification of enzymes. Main catalysis
mechanisms. Enzymatic kinetics. Steady state hypothesis, MichaelisMenten equation. Basic kinetic parameters: turnover number, specificity
constant, meaning and calculation method. Competitive, mixed and
incompetitive inhibition: kinetic aspects. Mechanisms of general
regulation of enzymes: covalent and non-covalent; allostery. Regulation
by proteolysis: serin-protease, cysteine-protease, aspartyl-protease,
metalloprotease3 Relationship structure-localization-function of biological
macromoleculesOrganization of cellular and subcellular membranes;
movement of lipids through the double layer. The fluid mosaic model. The
"lipid rafts" / lipid rafts. Post-translational modifications of proteins and
signals for localization. Signals of entry and retention in organelles or of
addressing to the plasma membrane. Proteins that bind O2: globins;
structure of the EME group. Structure and function of myoglobin: and
hemoglobin. Saturation curve. Allosteric T / R variants, cooperativity.
Equation and coefficient of Hill. Regulation of the affinity of Hb for its
ligand by: O2, CO2, H + and their role in the gaseous exchanges at the
pulmonary and tissue level. Role of 2,3 bisphosphoglycerate (BPG) in the
regulation of Hb affinity for O2. Molecular basis of thalassemia,
hemoglobinopathies and meteglobinemia. Proteins with recognition and
defense function: immunoglobulins: general classification, structure and
mechanisms of interaction with the antigen. Overview of the genetic
rearrangement that generates the variable regions of heavy and light
chains. Contractile structural unit: morphological and molecular
organization of muscle fiber, myofibrils and sarcomere. Biochemical
contraction mechanism: regulation of acto-myosin complex activity, role
of ATP and calcium ions Cytoskeletal proteins. Actin polymerization
mechanism, proteins that bind the actin and regulate its polymerization.
Microtubules: structure, mechanism of polymerization and intracellular
role. Molecular motors: chinesine and dineins. Structure and ATPdependent progress mechanism on the microtubule. Intermediate
filaments: functional characteristics and polymerization mechanism.
Extracellular matrix proteins: laminins, fibronectin, collagens, elastin.
Transport of molecules through the membranes: biochemistry of
vesicular traffic. Overview of the general mechanisms of endocytosis.
Bending mechanisms and cleavage of membranes. Endocytosis mediated
by clathrin and non-clathrin-dependent receptors. Transportation of
molecules through membranes: transporters and channels. General
mechanisms of transport through the membranes. Transport not
mediated; transporters and channels, facilitated transport, and active
transport. Ionic pumps. Co-transport and anti-charge systems. The ABC
carriers. Excitable membranes, action potentials and neurotransmission.
Voltage-dependent channels. Ionic channels controlled by ligands: the
acetylcholine channel receptor; channel desensitization mechanisms.

To be able to identify biological macromolecules, to catch the
interconnections between macromolecular structures, function and
regulation and to acquire independent judgment in the evaluation of
biochemical problems related to the structure and functioning of the
biomolecules within the cell and in the extracellular environment. Know
the mechanisms of enzyme activity and know how to solve simple
problems related to enzymatic kinetics. Possess the basic knowledge of
signal transduction and of cellular transport and mobility mechanisms