Learning objectives
The Course of Biochemistry aims to enable the student to know and understand the structure, organization and function of living matter in molecular terms also in order to allow the student the ability to use the knowledge and understanding gained in identifying problems associated with the structural chemistry and structure-function relationship; metabolism and its regulation; biological information pathways.
LEARNIG OUTCOMES:
The student at the end of the Course, using the knowledge of Organic Chemistry previously acquired, must demonstrate knowledge and understanding about:
-the interaction of drugs with biological macromolecules
-the effect of drugs on metabolism and its regulation
-the regulation of metabolism by drugs
-the disease as a result of a genetic modification of macromolecules; hypothetical therapy
In addition, students, applying the knowledge and understanding acquired, shall be able,even collaborating with other professionals, to help explain:
-the mechanism by which a drug or other health products acts in a biological process
-what are the molecular basis of diseases
-mechanism which regulate cellular homeostasis
-which food to allow normal growth, development and well-being.
The student must have sufficient technical language to explain molecular events occurring in the cell in health and/or disease.
The course of Applied Biochemistry is a part of teaching or course-integrated Biochemistry-Applied Biochemistry.
The Course aims to enable the student to know and understand the general principles of experimental biochemistry, biological materials, principles and equipment used for analytical and preparative purposes including for the purpose of allowing the student the ability to use the knowledge and understanding gained to understand the significance of biochemical investigation, discipline-based research, and appropriated the principles and methods normally used in biochemical laboratory.
LEARNIG OUTCOMES:
The student at the end of the Course, using the knowledge of Organic Chemistry previously acquired, must demonstrate knowledge and understanding about:
-material used in biochemical experiments
-preparative and analytical separation techniques
-spectroscopic techniques
-techniques based on biospecific interactions
In addition, students, applying the knowledge and understanding acquired, shall be able,even collaborating with other professionals, to help explain:
-how to investigate the mechanism of action of a drug
-investigate as to understanding the molecular basis of diseases
-how to study the properties of an enzyme marker of a disease
-how to measure an antigen in a biological fluid complex.
The student must have sufficient technical language to explain the various stages of extraction, separation,purification, molecular and functional characterizatio of macromolecules of biochemical interest.
Prerequisites
Basic knowledge of General Chemistry, Organic Chemistry,Cell Biology.
Course unit content
First part: Protein structure and function. Proteins of special physiological interest. Enzymes. Vitamins. Lipids. Biological membranes. Nucleotides and nucleic acids.
Second part: Bioenergetics, oxidative metabolism and hormonal regulation. Metabolism of carbohydrates: glycolysis, glycogen metabolism, gluconeogenesis, pentose phosphate pathway. Lipid metabolism. Amino acid metabolism. Tricarboxylic acid cycle. Oxidative phosphorylation. Metabolism of purine and pyrimidine nucleotides.Metabolism regulation.Signaling pathway.
Third part: Mechanisms of DNA duplication and RNA transcription . Protein synthesis.
The Applied Biochemistry course is part of the integrated course of Biochemistry-Applied Biochemistry.
First part:general criteria in biochemical experimentation. Biological materials. Second part:methods of separation and purification of proteins and other molecules of biochemical interest: centrifugation, salting out, dialysis, chromatography,electrophoresis. Third part: biochemical applications of visible and ultraviolet spectroscopy. Study of enzymatic activity. Immunochemical, radioisotope and radioimmunologic techniques. Potentiometric and polarographic techniques Overview of molecular biology.
Full programme
Introduction to the Biochemistry study
Amino acids, peptides
Three-dimensional protein structure
Myglobin and Hemoglobin
Antibody
Fibrous proteins
Enzymes and coenzymes
Lipids, membranes and transport
Nucleotides and nucleic acids
Bioenergetics and metabolic pathways
Carbohydrates metabolism
The citric acid cycle
Electron transport and ATP synthesis
Lipid metabolism
Amino acid metabolism
Nucleotide metabolism
Hormonal regulation and signaling pathways
DNA and RNA metabolism
Protein synthesis.
General principles of biochemical experimental investigation
Biological materials
Methods of separation and purification of proteins and other molecules of biochemical interest: centrifugation, salt fractionation, dialysis and ultrafiltration.
Chromatographic techniques. Principles and modes of chromatography. Chromatografic performance parameters. Adsorption chromatography; ion-exchange chromatography;molecular exclusion (gel filtration) chromatography; affinity chromatography; high performance liquid chromatography (HPLC);gas-liquid chromatography.
Electrophoretic techniques. General principles. Support media and detection methods. Electrophoresis of proteins and of nucleic acids. Isoelectric focusing. Capillary electrophoresis.
Spectroscopic techniques. Properties of electromagnetic radiation and interaction with matter. Ultraviolet and visible light spectroscopy. Spectrofluorimetry. Applications in biochemical analysis.
Enzyme assay and kinetic analysis.
Immunochemical techniques. Immunoglobulin structure. Production and purification of polyclonal and monoclonal antibodies. Immunoprecipitation . Labeling antibodies. Enzyme-
immunoassay.Immunoblotting.
Radioisotope techniques and radioimmunoassay (RIA).
Potenziometric and polarographic techniques
Bibliography
D.L.Nelson,M.M.Cox:'' I principi di Biochimica di Lehninger'';J.Berg,J.L.Tymoczko,L.Stryer:''Biochimica''; M.K.Campbell,S.O.Farrell”Biochimica”; D.Voet,J.G.Voet,C.W:Pratt:''Fondamenti di Biochimica'';T.M.Devlin:''Biochimica'';R.H.Garrett,C.M.Grisham:''Principi di Biochimica''; Siliprandi,Tettamanti:''Biochimica Medica".
K.Wilson,J.Walker:''Principi e tecniche di Biochimica e Biologia molecolare'';M.C.Bonaccorsi di Patti, R.Contestabile ,M.L.DiSalvo "Metodologie Biochimiche"2e;M.Maccarrone "Metodologie biochimiche e biomolecolari".
Teaching methods
Oral lesson frontal carried out with the help of communication tools.
Please refer to "Reference texts"useful for the preparation of exam.
Assessment methods and criteria
The verification of the achievement of the objectives set by the Integrated Course includes a written test with open answer with time available for 2 hours and 30 minutes.Through questions regarding the content will be determined whether the student has achieved the goal of understanding and knowledge.The answers to four questions will make it possible to ascertain whether the student has achieved the goal of applying the acquired knowledge. The first question will concern the structural chemistry and the structure-function relationship, the second the metabolism and the biological information pathways, the third regulation and/or deeping of metabolic pathways, the fourth the general principles of biochemical investigations and biological materials used, methods of separation and purification of proteins and other molecules of biochemical interest, the principles and application of spectroscopic techniques and immunochemical techniques. Each answer will be evaluated with a score from 0 to 30/30 praise. The final evaluation will consist of adding the vote obtained in the answer to each individual question and dividing by the number of questions.To pass the exam it is necessary to have a grade higher than eighteen in the Applied Biochemistry.
Other information
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