Biochemistry and Molecular Biology
A.Y. 2024/2025
Learning objectives
General aims of the course: (1) Knowledge of the molecular design of life, with particular emphasis on the main processes linked to energy production and storage, signal transduction and expression of genetic information, to allow the student to gain the scientific background necessary to understand physiological and pathological processes in animals presented in future courses; (2) Knowledge of the basic theory of colorimetric-based quantitative biological assay and of key topics related to recombinant DNA methodologies;(3) Knowledge of simple bioinformatic tools to allow the student to acquire key up-to-date information from reliable on-line bibliographic and scientific sources; (4)Undestanding the contribution of basic and applied research in veterinary science.
Expected learning outcomes
1- Knowledge and understanding. The student will acquire information concerning (a) the structure and function of the most relevant biomolecules, including macromolecules, (b) the main biological processes operating in animal cells, including the biological fate of the main components of nutrients, mechanisms of energy production and storage, molecular mechanisms of metabolic control and signal transduction and (c) expression of genetic information. The course is completed with seminars in which the previous information are used to describe in deeper details specific topics including three dimensional structure of proteins and related rationale drug design approaches, bioenergetics, oxidative stress, rumen biochemistry and recent developments in recombinant DNA technologies and proteomics.
2-Applying knowledge and understanding. The student will gain the necessary knowledge on cell and organism organization and function absolutely required in order to understand physio-pathological processes presented in a number of successive courses. Lectures are complemented with exercitative activities including exercises held in class collectively and practical laboratories, in which basic concepts of colorimetric assays are applied to the quantification of molecules of biological interest; the latter activities are also meant to be preparatory to the future course of Clinical Biochemistry. Student will acquire competences to obtain fundamental up-to-date information from bibliographic and scientific databanks
3- Making judgments. All information given in theoretical lectures and seminars is presented with an approach aimed at emphasizing the relevance of basic science researches in animal science and of the quantitative-based experimental methodology which is used to support any biological finding. Concerning laboratories activities, a critical discussion on all aspects of the activity is performed collectively in class. In addition, great emphasis is placed on the need to critically evaluate information from on-line sources
4-Communication. In order to learn how to work in group and communicate results efficiently, practical activities are performed in teams of two students and require the use of both manually and computer generated plots to present the results. The final examination consists in a written test with open answers, in which the student is also required to use an appropriate language, including proper scientific terminology, synthesis and completeness.
5- Life long learning skills. Knowledge of the main chemical components of organisms and food, knowledge of fundamental biological processes in organisms and ability in using tools to withdraw information from reliable on-line sources acquired during the course will allow life-long capacity to keep up-to-date on any topic of interest from scientific literature.
2-Applying knowledge and understanding. The student will gain the necessary knowledge on cell and organism organization and function absolutely required in order to understand physio-pathological processes presented in a number of successive courses. Lectures are complemented with exercitative activities including exercises held in class collectively and practical laboratories, in which basic concepts of colorimetric assays are applied to the quantification of molecules of biological interest; the latter activities are also meant to be preparatory to the future course of Clinical Biochemistry. Student will acquire competences to obtain fundamental up-to-date information from bibliographic and scientific databanks
3- Making judgments. All information given in theoretical lectures and seminars is presented with an approach aimed at emphasizing the relevance of basic science researches in animal science and of the quantitative-based experimental methodology which is used to support any biological finding. Concerning laboratories activities, a critical discussion on all aspects of the activity is performed collectively in class. In addition, great emphasis is placed on the need to critically evaluate information from on-line sources
4-Communication. In order to learn how to work in group and communicate results efficiently, practical activities are performed in teams of two students and require the use of both manually and computer generated plots to present the results. The final examination consists in a written test with open answers, in which the student is also required to use an appropriate language, including proper scientific terminology, synthesis and completeness.
5- Life long learning skills. Knowledge of the main chemical components of organisms and food, knowledge of fundamental biological processes in organisms and ability in using tools to withdraw information from reliable on-line sources acquired during the course will allow life-long capacity to keep up-to-date on any topic of interest from scientific literature.
Lesson period: Second semester
Assessment methods: Esame
Assessment result: voto verbalizzato in trentesimi
Single course
This course can be attended as a single course.
Course syllabus and organization
Single session
Responsible
Lesson period
Second semester
Prerequisites for admission
To take the exam, the student must have passed the compulsory preparatory examinations of Basic Sciences Propaedeutic to Veterinary Medicine
Assessment methods and Criteria
The examination takes place in a single written test consisting in 4 open questions, one for each of the following general subject: metabolism and its control, general biochemistry, molecular biology and the structure of a nucleic acid. Information concerning the specific topic comprised in each general subject is clearly indicated to students at the beginning of the course and can be found in the myARIEL site of the teacher (https://anegribbm.ariel.ctu.unimi.it/v5/home/Default.aspx). Students must complete the test in 2.5 hours. The overall final score of the test, beside correctness, takes into account completeness, clarity, synthesis and use of proper terminology.
Exams are in number of 8 in the Academic year and take place in the months of January, February, April June, July, September , October and November/December with the frequency set by the teaching board.
Exams are in number of 8 in the Academic year and take place in the months of January, February, April June, July, September , October and November/December with the frequency set by the teaching board.
Propedeutic Biochemistry
Course syllabus
Theoretical lectures (16 hours)
Nomenclature, structure and main reactions of biological relevance of hydrocarbons, alcohols, aldehydes/ketones, amines, carboxylic acid and their derivatives; esters and anhydrides containing deriving from phopshoric acid (3 hours)
Stereochemistry, conformation, geometric and otpical stereoisomery, hydrophobicity and their relevance in biology (1 hour)
Structure and main biological roles of carbohydrates: aldoses and ketoses; monosaccharides (glucose, fructose, galctose, ribose); O- and N- glycosidic bonds; disaccharides (lactose, maltose); homo- and hetero-glycans (starch, cellulose, structural polyisaccharides) (3 hours)
Structure and main biological roles of amino acids and proteins: proteic and non-proteic amino acids; classification of amino acids based on chemical properties of the side chain; essential and non-essential amino acids; peptide bond; peptides and proteins; glycoproteins and proteoglycans; amino acid composition of a protein and amino acid content of food (4 hours)
Structure and main biological roles of lipids: fatty acids. Omega-9, -6, -3 unsaturated fatty acids; triacylglycerols, phospholipids. steroids, lipopolysaccharides (2 hours)
Structure and main biological roles of nucleosides and nucleotides; free nucleotides as coenzymes and signalling molecules; vitamins (3 hours)
Practical lectures (16 hours)
Exercises on compound nomenclature and main organic chemistry reactions of biological interest (6 hours) (classroom)
Exercises on oxidation number of biochemical compounds and redox-reactions (1 hours) (classroom)
Examples of stereochemistry and 3 dimensional structure of molecules using atomic models and material available on-line (1 hour) (classroom)
Bioenergetics: energy changes associated with biologically relevant chemical reactions and related exercises (3 hours) (classroom)
Seminar: primary, secondary, tertiary and quaternary structure of proteins and their effect on biological properties (2 hours) (classroom)
Computer based practical activity: use of on-line databases and software to described the structure-function relationship in models proteins and understand the basic of the Rationale Drug Design approach (3 hours) (classroom, each student uses his own computer).
Nomenclature, structure and main reactions of biological relevance of hydrocarbons, alcohols, aldehydes/ketones, amines, carboxylic acid and their derivatives; esters and anhydrides containing deriving from phopshoric acid (3 hours)
Stereochemistry, conformation, geometric and otpical stereoisomery, hydrophobicity and their relevance in biology (1 hour)
Structure and main biological roles of carbohydrates: aldoses and ketoses; monosaccharides (glucose, fructose, galctose, ribose); O- and N- glycosidic bonds; disaccharides (lactose, maltose); homo- and hetero-glycans (starch, cellulose, structural polyisaccharides) (3 hours)
Structure and main biological roles of amino acids and proteins: proteic and non-proteic amino acids; classification of amino acids based on chemical properties of the side chain; essential and non-essential amino acids; peptide bond; peptides and proteins; glycoproteins and proteoglycans; amino acid composition of a protein and amino acid content of food (4 hours)
Structure and main biological roles of lipids: fatty acids. Omega-9, -6, -3 unsaturated fatty acids; triacylglycerols, phospholipids. steroids, lipopolysaccharides (2 hours)
Structure and main biological roles of nucleosides and nucleotides; free nucleotides as coenzymes and signalling molecules; vitamins (3 hours)
Practical lectures (16 hours)
Exercises on compound nomenclature and main organic chemistry reactions of biological interest (6 hours) (classroom)
Exercises on oxidation number of biochemical compounds and redox-reactions (1 hours) (classroom)
Examples of stereochemistry and 3 dimensional structure of molecules using atomic models and material available on-line (1 hour) (classroom)
Bioenergetics: energy changes associated with biologically relevant chemical reactions and related exercises (3 hours) (classroom)
Seminar: primary, secondary, tertiary and quaternary structure of proteins and their effect on biological properties (2 hours) (classroom)
Computer based practical activity: use of on-line databases and software to described the structure-function relationship in models proteins and understand the basic of the Rationale Drug Design approach (3 hours) (classroom, each student uses his own computer).
Teaching methods
The course consists of theoretical and practical lectures. The latter comprise, in addition to exercizes held in the classroom on basic structures and main reactivity of organic compounds of biological interest, seminars and computer-based practical training on the use of biological databases and softwares for the analysis of structure-function relationship in proteins available on-line.
Teaching Resources
For organic chemistry topics: any secondary school Chemistry book; any basic level chemistry website
Power Point slides on Ariel web-site (https://anegribbm.ariel.ctu.unimi.it/v5/home/Default.aspx)
Suggested textbook:
-D.L. Nelson M.M. Cox Introduzione alla biochimica di Lehninger (Zanichelli)
or
-Campbell Farrell Biochimica (Edises)
Power Point slides on Ariel web-site (https://anegribbm.ariel.ctu.unimi.it/v5/home/Default.aspx)
Suggested textbook:
-D.L. Nelson M.M. Cox Introduzione alla biochimica di Lehninger (Zanichelli)
or
-Campbell Farrell Biochimica (Edises)
Biochemistry
Course syllabus
Theoretical lectures (32 h):
Structure and function of membranes. Transport across membranes (2 h)
Collagen (1 h)
Oxygen-transporting proteins: myoglobin and hemoglobin (3 h)
Lipoproteins, fatty acid binding proteins (1 h)
Enzymes and co-enzymes (2 h)
Molecular mechanisms of digestion, absorption and transport of the main nutritionally relevant classes of compounds (2 h)
Metabolism of carbohydrates (4 h)
Metabolism of triacylglycerols, fatty acids, ketone bodies, Overview of metabolism of cholesterol (3 h)
Krebs cycle and oxidative phosphorylation (3 h)
Metabolism of amino acids: amino acid degradation and the urea cycle, overview of amino acid biosynthesis of nucleotide metabolism (3 h)
Structure and function of nucleic acids (1 h)
DNA replication (2 h)
Transcription (2 h)
Genetic code, translation, post-translational modifications (3 h)
Practical laboratories and seminars (16 h)
Seminar: Mechanisms of enzyme regulation (2 h) (class)
Seminar: Molecular basis of oxidative stress (1 h) (class)
Seminar: Anaerobic metabolism, fermentation and rumen metabolism (2 h) (class)
Theory of spectrophotometrical determination of biological compounds (1 h) (class)
Colorimetrical determination of glucose, total protein content and alkaline phosphatase (4 h, 2 h practical laboratory+ 2 h discussion of results in class)
Seminar: Recombinant DNA and molecular biology applications: recombinant proteins and Polymerase Chain Reaction (2 h) (class)
Seminar: Gene expression mechanisms (1 h) (class)
Seminar: Proteomics (1 h) (class)
Computer laboratory: use of (a) Excel to analyze and plot experimental data obtained in the practical laboratory; (b) Proteomic databank searches as tolls to obtain up-to-date information on biological relevant information on proteins (structure, expression, biological function, involvement in physiological and pathological conditions); (c) PubMed as a tool to analyze/review scientific literature (including steps to download non open-access articles) (2 h) (computer lab)
Structure and function of membranes. Transport across membranes (2 h)
Collagen (1 h)
Oxygen-transporting proteins: myoglobin and hemoglobin (3 h)
Lipoproteins, fatty acid binding proteins (1 h)
Enzymes and co-enzymes (2 h)
Molecular mechanisms of digestion, absorption and transport of the main nutritionally relevant classes of compounds (2 h)
Metabolism of carbohydrates (4 h)
Metabolism of triacylglycerols, fatty acids, ketone bodies, Overview of metabolism of cholesterol (3 h)
Krebs cycle and oxidative phosphorylation (3 h)
Metabolism of amino acids: amino acid degradation and the urea cycle, overview of amino acid biosynthesis of nucleotide metabolism (3 h)
Structure and function of nucleic acids (1 h)
DNA replication (2 h)
Transcription (2 h)
Genetic code, translation, post-translational modifications (3 h)
Practical laboratories and seminars (16 h)
Seminar: Mechanisms of enzyme regulation (2 h) (class)
Seminar: Molecular basis of oxidative stress (1 h) (class)
Seminar: Anaerobic metabolism, fermentation and rumen metabolism (2 h) (class)
Theory of spectrophotometrical determination of biological compounds (1 h) (class)
Colorimetrical determination of glucose, total protein content and alkaline phosphatase (4 h, 2 h practical laboratory+ 2 h discussion of results in class)
Seminar: Recombinant DNA and molecular biology applications: recombinant proteins and Polymerase Chain Reaction (2 h) (class)
Seminar: Gene expression mechanisms (1 h) (class)
Seminar: Proteomics (1 h) (class)
Computer laboratory: use of (a) Excel to analyze and plot experimental data obtained in the practical laboratory; (b) Proteomic databank searches as tolls to obtain up-to-date information on biological relevant information on proteins (structure, expression, biological function, involvement in physiological and pathological conditions); (c) PubMed as a tool to analyze/review scientific literature (including steps to download non open-access articles) (2 h) (computer lab)
Teaching methods
The course consists of theoretical lectures, with the aid of on-line scientific movies in order to describe the complex molecular events leading to nucleic acids and protein synthesis, practical lectures and seminars on specific topics of interest. Practical activities consist in the execution of biological assays in teaching laboratories and in computer-based evaluation of experimental results and database searching.
Teaching Resources
Suggested textbook:
-D.L. Nelson M.M. Cox Introduzione alla biochimica di Lehninger (Zanichelli)
or
-Campbell Farrell Biochimica (Edises)
Power Point slides on myAriel web-site https://myariel.unimi.it/course/view.php?id=2098
-D.L. Nelson M.M. Cox Introduzione alla biochimica di Lehninger (Zanichelli)
or
-Campbell Farrell Biochimica (Edises)
Power Point slides on myAriel web-site https://myariel.unimi.it/course/view.php?id=2098
Biochemistry
BIO/10 - BIOCHEMISTRY - University credits: 5
Practicals: 16 hours
Lessons: 32 hours
Lessons: 32 hours
Professor:
Negri Armando
Shifts:
Professor:
Negri Armando
1 TURNO PER TUTTI GLI STUDENTI DA 14 ORE
Professor:
Negri Armando2 TURNO PER GRUPPI DI STUDENTI DA 2 ORE
Professor:
Negri Armando3 TURNO PER GRUPPI DI STUDENTI DA 2 ORE
Professor:
Negri Armando4 TURNO PER GRUPPI DI STUDENTI DA 2 ORE
Professor:
Negri Armando5 TURNO PER GRUPPI DI STUDENTI DA 2 ORE
Professor:
Negri Armando
Propedeutic Biochemistry
BIO/10 - BIOCHEMISTRY - University credits: 3
Practicals: 16 hours
Lessons: 16 hours
Lessons: 16 hours
Professor:
Negri Armando
Shifts:
Professor:
Negri Armando
1 TURNO PER TUTTI GLI STUDENTI DA 16 ORE
Professor:
Negri ArmandoProfessor(s)