Biochemistry
Code: 102662Credits: 8
| Degree programme | Type | Course |
|---|---|---|
| Veterinary Medicine | FB | 1 |
Contact lecturer
- Name :
- Maria Jose Docampo Garcia
- Email :
- mariajose.docampo@uab.cat
Teaching staff
- Néstor Gomez Trias
- Joaquín Ariño Carmona
- Asier Gonzalez Sevine
- Antonio Casamayor Gracia
Group languages
You can consult this information at the end of the document.
Prerequisites
There are no official prerequisites, but it is convenient that the student has assimilated the basic principles of chemistry and biochemistry.
Objectives
This subject should enable students to understand that the biological processes of animals have a chemical basis and can be explained in these terms.
Students should understand the structural foundations of these processes, as well as the structure-function relationship in the different types of biological compounds: carbohydrates, lipids, proteins and nucleic acids.
Likewise, students should be familiar with the fundamentals of metabolism, enabling them to understand the biochemical basis of physiology and pathology, with special emphasis on animal species of veterinary interest.
Finally, students shoud understand the molecular basis of genetic information transmission and its regulation.
The specific learning objectives are to know and understand:
- The basic elements of biological chemistry: functional groups, chemical equilibrium, principles of bioenergetics, enzyme kinetics, redox potential, isomers and stereoisomers.
- The structure and function of proteins, carbohydrates, lipids, nucleotides and vitamins.
- The structure of nucleic acids and the processes of replication, transcription, translation and regulation of gene expression.
- The energy metabolism of carbohydrates.
- The metabolism of lipid reserves, lipoproteins, cholesterol and complex lipids.
- The metabolism of nitrogenous compounds: amino acids, porphyrins and nucleotides.
- The main mechanisms of metabolism integration and the molecular basis of metabolic adaptations and disorders.
- The fundamentals and applications of the main biochemical techniques and methodologies.
Practical activities related to this discipline are carried out in the Integrated Laboratory subject.
Learning outcomes
- Analyse, synthesise and resolve problems and make decisions.
- Seek and manage information related with professional activity
- Describe the main functional groups of biological interest and their chemical properties.
- Recognise the main types of organic reactions and apply these concepts to biological processes.
- Explain the basic structures of the main biological molecules.
- Describe the basic principles of kinetic and enzymatic regulation.
- Distinguish the mechanisms for transmitting and regulating the genetic information pf a cell.
- Explain the main metabolic pathways.
- Integrate different metabolic elements in a global overview of the organism.
- Establish the molecular basis of different physiological and pathological processes.
- Identify the fundaments for the determination of biochemical parameters of diagnostic interest in the laboratory and evaluate their relevance individually and in profiles in the diagnosis.
Contents
PART 1. THE CHEMISTRY OF LIVING BEINGS
Unit 1.- Introduction to the chemistry of living beings. Carbon bonds: simple and multiple. Classification of organic compounds: degree of oxidation and functional groups of biological interest. Cis-trans isomerism. Stereochemistry concepts. Enantiomers Chiral compounds and their importance in living systems. Diastereoisomers. Properties of water and importance of the aqueous medium for living organisms.
Unit 2.- Aliphatic and aromatic hydrocarbons. Alcohols, ethers, epoxides and phenols. Carbonyl compounds: aldehydes and ketones. Carboxylic acids and their derivatives: esters, amides, chlorides and acid anhydrides. Nitrogen organic compounds: Amines, amides and nitriles. Heterocyclic compounds with nitrogen, oxygen and sulphur.
Unit 3.- Chemical equilibrium. Equilibrium constant. Acid-base balance. pH and buffer solutions. Its importance in biology.
Unit 4.- Basic concepts of thermodynamics. Bond energies. Free energy (Gº) and spontaneous processes. Relationship between ΔGº and Keq. The ATP as an energy currency. Structural bases of the free energy change during the hydrolysis of ATP. Transfer of phosphate groups.
Unit 5.- Oxidation-reduction reactions. Redox pairs. Electrode potentials and prediction of redox reactions. Nernst equation. Importance of redox reactions in biochemistry.
Unit 6.- Constituents of proteins: amino acids. Structure and properties.
Unit 7.- The amino acid sequence of proteins. The peptide bond. The primary structure of proteins. Peptide sequencing.
Unit 8.- Three-dimensional structure of proteins. Secondary structure The α-helix and the β sheet. Tertiary structure. Quaternary structure. Structural domains. Native conformation and denaturation.
Unit 9.- Fibrous proteins. α-keratin, fibroin and collagen
Unit 10.- Oxygen-binding proteins. Structure of myoglobin and hemoglobin. The oxygen-binding centre. Cooperativity andallosterism. Allosteric effectors. Abnormal hemoglobins
Unit 11.- Catalytic proteins: enzymes. General properties Classification. Substrates and cofactors. Isozymes. Enzymatic catalysis.
Unit 12.- Enzyme kinetics. The Michaelis-Menten equation. Meaning of Km y Vmax. Effects of pH and temperature on enzyme activity. Enzymatic inhibition. Main mechanisms of catalysis.
Unit 13.- Mechanisms of regulation of enzymatic activity: Regulation of enzyme concentration. Allosteric enzymes. Reversible covalent modification. Protein-protein interactions. Changes in subcellular localization. Irreversible covalent modification (proteolysis)
Unit 14.- Vitamins. Structure, function, requirements and vitamin deficiency.
PART 2. METABOLISM AND METABOLIC REGULATION
Unit 15.- Study of the regulation of metabolic pathways. Localization of regulation sites. Study of the properties of the enzymes involved. Crossing points. Development and verification of a theory of regulation.
Unit 16. Biochemical study of carbohydrates. Generalities. Families of monosaccharides. Natural oligosaccharides. Storage and structural polysaccharides.
Unit 17.- Glycolysis. Overview and phases. Stages of the process of the formation of pyruvate from glucose.
Unit 18.- Formation of acetyl CoA from pyruvate and tricarboxylic acid cycle. Anaplerotic pathways. Glyoxylic acid cycle. Synthesis and degradation of disaccharides. Metabolic pathways of fructose and galactose.
Unit 19.- Oxidation-Reduction and electronic transport. Redox potentials and free energy change. Electronic transport route: the respiratory chain. Inhibitors The mitochondria and oxidative phosphorylation. Coupling of oxidative phosphorylation to electronic transport. The mechanism of oxidative phosphorylation.
Unit 20.- Lactate formation and gluconeogenesis. Use of energy by the muscle. Anaerobic glycolysis. Lactate destination. Gluconeogenesis. Other precursors. Distinctive reactions of gluconeogenesis.
Unit 21.- Pentose phosphate pathway. Obtaining reducing power. Glucuronic acid pathway.
Unit 22.- Metabolism of glycogen. Glycogen as a storage form of glucose. The degradation and synthesis of glycogen and its control.
Unit 23.- Biochemical study of lipids. Fatty acids. Waxes. Triglycerides. Phosphoglycerides. Sphingolipids and glycolipids. Cholesterol.
Unit 24.- Oxidation of fatty acids. Mobilization of lipid reserves. b-oxidation. Ketone body’s metabolism.
Unit 25.- Biosynthesis of storage lipids. Biosynthesis of saturated fatty acids. The formation of malonyl-CoA. The fatty acid synthetase complex.
Unit 26.- The biosynthesis of cholesterol and derivatives. Regulation of cholesterol biosynthesis. Bile acids and sex hormones.
Unit 27.- Digestion and absorption of lipids. Lipoproteins. Composition and metabolism.
Unit 28.- Metabolism of structural lipids. Phosphoglycerides. Sphingolipids: sphingomyelin, cerebrosides and gangliosides. Phosphatidylinositol cycle. IP3 synthesis.
Unit 29.- Degradation of amino acids. Release and elimination of nitrogen. Deamination and transamination. Urea cycle.
Unit 30.- Catabolism of the carbon skeletons of amino acids. Ketogenic and gluconeogenic amino acids. The integration of the chains in the different metabolic pathways. Aminoacid diseases. The reserve of monocarbonate groups and their relation to amino acid metabolism and its regulation: folic acid derivatives and S-adenosylmethionine.
Unit 31. - Nitrogen fixation, overview of amino acid biosynthesis and its regulation. Essential and not essential amino acids.
Unit 32.- Structure and metabolism of nucleotides. Nucleotide biosynthesis: purines and pyrimidines. Biosynthesisofdeoxyribonucleotides. Degradation of purines and pyrimidines.
Unit 33.- Metabolic integration.
PART 3. REPLICATION, TRANSCRIPTION, TRANSLATION AND THEIR REGULATION
Unit 34.- Nucleic acids. DNA and its structure. The equivalence of bases. The double helix. Nucleosomes.
Unit 35.- DNA: genetic role and replication. Semiconservative replication. DNA polymerases. Okazaki fragments. DNA replication: initiation, elongation and termination. DNA repair
Unit 36.- Transcription and regulation of gene expression in prokaryotes. Promoters of prokaryotes. Start and end of the synthesis. Lactose operon.
Unit 37.- Transcription and regulation of gene expression in eukaryotes. Promoters and enhancers. Transcription factors. Chemical modifications of histones and DNA.
Unit 38.- mRNA processing in eukaryotes. Introns and splicing. Post-transcriptional modifications of rRNA and tRNA.
Unit 39.- The genetic code. The nature of the code and its main characteristics. The triplets of bases. The transfer RNA as adapter in the protein synthesis.
Unit 40.- Proteins synthesis . Activation of amino acids. Characteristics of aminoacyl tRNA synthetases. Direction of the synthesis. Initiation, elongation and termination. Introduction to the synthesis of proteins in eukaryotes.
SEMINARS
Chromatographic techniques.
Electrophoresis.
Metabolites of clinical interest.
Enzymes of clinical interest.
Porphyrin metabolism. Porpphyrias and jaundice.
Cell signalling.
Biochemical aspects of animal production diseases.
Recombinant DNA techniques.
The theoretical contents of parts 1 and 2, as well as 7 seminars, correspond to the first semester. The contents of part 3 and the last seminar correspond to the second semester.
Learning activities and methodology
| Title | Hours | ECTS | Learning outcomes |
|---|---|---|---|
| Study and bibliographic inquiry | 99 | 3.96 | 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 |
| Theoretical classes | 58 | 2.32 | 3, 4, 5, 6, 7, 8, 9, 10, 11 |
| Preparation of self-learning work | 30.5 | 1.22 | 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 |
| Seminars and discussion of problems | 8 | 0.32 | 1, 3, 4, 5, 6, 7, 8, 9, 10, 11 |
The methodology used in this subject combines theory lectures, seminars, and active self-learning by students on topics of interest.
• In-person theory lectures, where the teaching staff presents the most relevant aspects of each topic. Students will have access to the materials on the Virtual Campus.
• Seminars and problem discussion, with the presentation of specific topics by the teaching staff and discussion in small groups. Seminars will be held in person.
• Independent student work (self-learning), individually or in groups, for the study and preparation of topics proposed by the teaching staff. This work involves searching for and selecting information from various scientific sources. The resulting presentations will be public, must include multimedia materials and ICT support, and will be followed by discussion of the topic. The presentations will take place during the second semester and will be held in person.
In this subject, the use of Artificial Intelligence (AI) technologies is permitted as a support tool in the development of coursework, provided that the final result reflects a significant contribution from the student in terms of analysis and personal reflection. Students must explicitly indicate which parts of the work were generated with the support of this technology, specify the tools used, and include a critical reflection on how they influenced both the process and the final outcome. Lack of transparency in the use of AI will be considered a breach of academic integrity and may result in a penalty on the activity grade or more severe sanctions in serious cases.
Assessment
Continuous assessment activities
| Title | Weight | Hours | ECTS | Learning outcomes |
|---|---|---|---|---|
| Partial examinations | 80% | 2 | 0.08 | 3, 4, 5, 6, 7, 8, 9, 10, 11 |
| Presentation and discussion of self-learning work | 20% | 2.5 | 0.1 | 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 |
The assessment system is structured in two modules:
- Module 1. Theory and seminars (80% of the final grade)
- Module 2. Self-learning work (20% of the final grade)
The final grade is obtained from the weighted sum of these two modules, in accordance with the criteria detailed below.
CONTINUOUS ASSESSMENT
Module 1. Theory and seminars
The assessment system consists of multiple-choice test exams. Three partial exams will be held throughout the course, corresponding to the parts described in the "Course Contents". Each exam will consist of approximately 25 questions, including both theory and seminar content.
The weight of each partial in the final grade is as follows:
- Partial 1: 25%
- Partial 2: 35%
- Partial 3: 20%
Passing the partial exams in continuous assessment:
Each partial is assessed independently and is passed with a grade equal to or higher than 5.0. However, it is possible to compensate for a failed partial by calculating the weighted average with the grades of the other partials and the self-learning component, only if one of the following conditions is met:
- One single partial is failed with a grade equal to or higher than 4.0, or
- Two partials are failed with grades equal to or higher than 4.5 in both.
If the weighted average is equal to or higher than 5.0, the course will be considered passed. Otherwise, students must sit only for the failed partials (those with a grade lower than 5.0) in the final exam.
Final exam:
The final exam will consist of independent tests for each partial. Students will only be examined on the partials not passed. To pass the course at this stage:
- If one single partial is retaken: minimum grade of 4.0 in the partial and a final weighted average equal to or higher than 5.0.
- If two or more partials are retaken: it is accepted that one partial has a grade equal to or higher than 4.0 if the remaining two have a minimum grade of 5.0, or that two partials have a grade equal to or higher than 4.5 if the third has a minimum grade of 5.0. The final weighted average must be equal to or higher than 5.0.
The course will not be considered passed if:
- Any partial has a grade lower than 4.0.
- All three partials have grades lower than 5.0.
Students, regardless of the grades obtained in the partial exams, may choose to take a final exam covering the entire syllabus to improve their grade. In this case, the final grade will be the one obtained in this last exam.
Students who have not participated in any of the assessable activities will be graded as 'Not assessed'.
Module 2. Self-learning
The presentation of the work will be assessed, considering both the oral presentation and the ability to discuss the topic. It has a weight of 20% in the final grade.
The completion of the self-learning work, as well as attendance and participation in its presentation session, are mandatory. Students who do not give the presentation will not be able to pass the course.
SINGLE ASSESSMENT
Single assessment involves passing the two modules, as indicated in the course guide:
- Module 1 (80%): a global exam including all theoretical content, held on the same day on which the rest of the students take the third partial exam. The resit exam will take place on the same date as for the rest of the students. The assessment criteria, as well as the specific weight of each partial in the final grade, are those stated in the course guide for continuous assessment.
- Module 2 (20%): oral presentation and individual defence of a work. The student must attend the presentation on the day assigned to their group. The oral presentation will be carried out individually on the day of the single assessment. This activity is mandatory.
Any irregularity committed during an assessment activity (academic fraud, plagiarism, or improper use of AI, unless such use is expressly authorised in the course guide), which may lead to a significant variation in the grade, will result in that activity being graded 0. If the course guide establishes a minimum grade in that activity as a requirement to pass the subject, or if several irregularities occur across assessment activities within the same subject, the final grade for the subject will be 0. In addition, disciplinary proceedings may be initiated against any student who engages in any of these irregularities.
Bibliography
Nelson, D.L., & Cox, M.M. Lehninger Principios de Bioquímica. 7a edición. Ed. Omega. (2018).
Nelson, D.L., & Cox, M.M. Lehninger Principies of Biochemistry. Eighth Edition. (2021).
Stryer, L., Berg, J. M., & Tymoczko, J. L. Bioquímica. 7ª edición. Ed. Reverté. (2013).
Stryer, L., Berg, J., Tymoczko, J & Gatto, G. Biochemistry. Ninth Edition (2019).
Software
No specific software is used.
Course groups and languages
The information provided is provisional until November 30. After this date, you will be able to consult the language of each group through this link. To access the information, you will need to enter the course CODE
| Type of teaching | Group | Language | Semester | Shift |
|---|---|---|---|---|
| (TE) Theory | 1 | Catalan/Spanish | annual | morning-mixed |
| (PAUL) Classroom practices | 1 | Catalan/Spanish | annual | morning-mixed |
| (TE) Theory | 2 | Catalan/Spanish | annual | morning-mixed |
| (PAUL) Classroom practices | 2 | Catalan/Spanish | annual | morning-mixed |
| (PAUL) Classroom practices | 3 | Catalan/Spanish | annual | morning-mixed |