Biochemistry I
Code: 103266 ECTS Credits: 6| Degree | Type | Year |
|---|---|---|
| 2501925 Food Science and Technology | FB | 1 |
Contact
- Name:
- Asier Gonzalez Sevine
- Email:
- asier.gonzalez@uab.cat
Teachers
- Anna Maria Bassols Teixido
- Antonio Jesus Casamayor Gracia
Teaching groups languages
You can view this information at the end of this document.
Prerequisites
There are no official prerequisites. However, it is advisable to review the basic contents of Biology and Chemistry of the first semester and the Baccalaureate.
Objectives and Contextualisation
This subject should allow students to understand that biological processes, especially those related to food and metabolism, have a chemical basis and that can be explained in these terms.
Students must understand the structural bases of these processes, as well as the structural bases that explain the function in the different types of biological compounds: carbohydrates, lipids, proteins, vitamins, and trace elements, and nucleic acids.
Likewise, students must understand the molecular basis of the transmission of genetic information and its regulation, as well as its applications in food biotechnology.
The specific goals are to identify and understand:
- 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 foundations and applications of the main Biochemistry and Molecular Biology techniques and methodologies.
With a special focus on Food Science and Technology.
Competences
- Adopt an ethical stance and attach importance to quality in work.
- Analyse, summarise, resolve problems and make professional decisions.
- Apply knowledge of the basic sciences to food science and technology.
- Apply the scientific method to resolving problems.
- Communicate effectively with both professional and non-professional audiences, orally and in writing, in the first language and/or in English.
- Develop individual learning strategies and planning and organisation skills.
- Display knowledge of nutrients, of their bioavailability and function in the organism, and the bases of nutritional balance.
- Display knowledge of the physical, chemical, biochemical and biological properties of raw materials and foods.
- Search for, manage and interpret information from different sources.
- Stay abreast of new knowledge, adapt to new situations and develop creativity.
- Use IT resources for communication, the search for information within the field of study, data processing and calculations.
Learning Outcomes
- Adopt an ethical stance and attach importance to quality in work.
- Analyse, summarise, resolve problems and make professional decisions.
- Apply the fundamental principles and the applications of biochemistry to food biotechnology.
- Apply the scientific method to resolving problems.
- Communicate effectively with both professional and non-professional audiences, orally and in writing, in the first language and/or in English.
- Describe mechanisms of transmission and regulation of genetic information in the cell.
- Describe the reactions of reaction, kinetics and enzyme regulation.
- Develop individual learning strategies and planning and organisation skills.
- Establish the metabolic role of vitamins, oligoelements and other essential nutrients.
- Explain the structures and properties of the principal biological molecules.
- Search for, manage and interpret information from different sources.
- Stay abreast of new knowledge, adapt to new situations and develop creativity
- Use IT resources for communication, the search for information within the field of study, data processing and calculations.
Content
THEORY LECTURES
PART 1. THE CHEMISTRY OF LIFE
Unit 1. Introduction to the chemistry of living organisms. Biomolecules. Properties of water and importance of the aqueous environment for living organisms.
Unit 2. Constituents of proteins: amino acids. Structure and properties.
Unit 3. Amino acid sequence of proteins. The peptide bond. The primary structure of proteins. Sequencing of peptides.
Unit 4. Three-dimensional structure of proteins. Secondary structure. The α-helix and the β-sheet. Tertiary structure. Quaternary structure. Structural domains. Native conformation and denaturalization.
Unit 5. Fibrous proteins. α-keratin, collagen, and others.
Unit 6. Oxygen-transport proteins. Structure of myoglobin and hemoglobin. The oxygen binding center. Cooperativity and allosterism. Allosteric effectors.
Unit 7. Catalytic proteins: enzymes. General properties. Classification. Substrates and coenzymes or cofactors. Isozymes. Enzymatic catalysis.
Unit 8. Enzyme kinetics. The Michaelis-Menten equation. Meaning of Km and Vmax. Effects of pH and temperature on enzymatic activity. Enzyme inhibition. Main mechanisms of catalysis.
Unit 9. Mechanisms of regulation of enzymatic activity. Regulation of enzyme concentration. Allosteric enzymes. Reversible covalent modification. Protein-protein interaction. Changes in subcellular localization. Irreversible covalent modification (proteolysis).
Unit 10. Vitamins and trace elements. Structure, function, requirements and avitaminosis.
Unit 11. Biochemical study of carbohydrates. Generalities. Families of monosaccharides. Natural oligosaccharides. Reserve polysaccharides and structural polysaccharides.
Unit 12. Biochemical study of lipids. Fatty acids. Triglycerides. Phosphoglycerides. Sphingolipids and glucolipids. Cholesterol
Unit 13. Nucleotides and derivatives. Purines and pyrimidines and their nucleotides. Nucleotides as enzymatic cofactors. Cyclic AMP.
PART 2. REPLICATION, TRANSCRIPTION, PROTEIN SYNTHESIS (TRANSLATION) AND THEIR REGULATION
Unit 14. Nucleic Acids. DNA and its structure. Nucleotide equivalence. Double helix. Nucleosomes.
Unit 15. DNA replication. Semiconservative replication. DNA polymerases. Okazaki fragments. DNA replication: initiation, elongation, and termination. DNA repair.
Unit 16. RNA and transcription. RNA polymerase and synthesis of RNAs. Prokaryotic and eukaryotic promoters. Post-transcriptional modifications of rRNA and tRNA. Processing of mRNA in eukaryotes. Introns and splicing.
Unit 17. Genetic code. The nature and main features of the genetic code. Nucleotide triplets. tRNA as an adapter in protein synthesis.
Unit 18. Protein synthesis. Activation of amino acids. Characteristics of aminoacyl-tRNA synthetases. Initiation, elongation, and termination. Introduction to protein synthesis in eukaryotes.
Unit 19. Control of gene expression. Gene induction and repression. lac operon. Control of gene expression in eukaryotes.
Unit 20. Introduction to food biotechnology. Introduction to recombinant DNA techniques. Biotechnological applications of bacteria, yeasts, plants and animals. Analytical techniques: PCR, antibodies, biosensors.
LABORATORY PRACTICAL SESSIONS
Practical session 1. Separation of a mixture of amino acids by ion exchange chromatography and identification by thin layer chromatography.
Practical session 2. Enzymes: determination of the Km.
Practical session 3. Computer room: Bibliographic databases and research articles.
Practical session 4. (2 days). Applications of PCR to food biotechnology.
SEMINARS
Seminar 1. Protein purification techniques.
Seminar 2. Spectrophotometric techniques.
Seminar 3. Enzymatic analysis.
Seminar 4. Discussion of a scientific article.
Seminar 5. PCR, cloning, and expression of recombinant proteins.
Seminar 6. DNA sequencing, microarrays, RNA-seq.
Activities and Methodology
| Title | Hours | ECTS | Learning Outcomes |
|---|---|---|---|
| Type: Directed | |||
| Laboratory practical sessions | 12 | 0.48 | 2, 4, 3, 1, 8, 10 |
| Seminars and problem solving | 6 | 0.24 | 2, 4, 3, 9, 10 |
| Theory lectures | 31 | 1.24 | 2, 4, 3, 1, 7, 6, 9, 10 |
| Type: Supervised | |||
| Self-learning preparation | 22.5 | 0.9 | 3, 1, 11, 5, 7, 6, 8, 9, 10, 13 |
| Type: Autonomous | |||
| Study and bibliographic search | 74 | 2.96 | 2, 4, 3, 11, 7, 6, 8, 9, 10, 13 |
The methodology of the learning process combines i) theoretical classes where the teachers expose the most relevant aspects of each subject with ii) active self-learning by the students on topics of interest. The subject is based on the following activities:
- Presential lectures with ICT support explaining the basic concepts of the subject. Kahoot will be used as a game-based learning tool.
- Seminars and problem solving-oriented lectures: Presentation by the teachers of specific topics and discussion in small groups.
- Laboratory practical sessions: Acquisition of work skills in the laboratory and experimental understanding of concepts explained in pressential classes and seminars.
- Autonomous work of the students, individually or in groups, for the preparation of topics proposed by the teachers or by the students. This work involves the search and selection of information in various sources of scientific databases. Presentations are public, must include multimedia material and ICT support, and are followed by a discussion.
Some lectures may be given as flipped classes, i.e., students will need to follow the corresponding video for the topic during non-presential hours, and during the class time problems will be solved and doubts will be addressed.
Questions and/or activities can be proposed through the moodle classroom (campus virtual).
Annotation: Within the schedule set by the centre or degree programme, 15 minutes of one class will be reserved for students to evaluate their lecturers and their courses or modules through questionnaires.
Assessment
Continous Assessment Activities
| Title | Weighting | Hours | ECTS | Learning Outcomes |
|---|---|---|---|---|
| Exam of laboratory practices | 10 | 0 | 0 | 2, 4 |
| Partial and final exams | 70 | 2 | 0.08 | 2, 3, 1, 7, 6, 8, 9, 10 |
| Presentation and discussion of self-learning project | 20 | 2.5 | 0.1 | 2, 4, 3, 11, 5, 7, 6, 9, 10, 12, 13 |
The maximum score is 10 points. Students will pass the subject with an overall score of 5.0 or higher.
The evaluation system is organized in three modules. The final qualification is obtained with the sum of the qualifications of the different modules, with the conditions described below.
• Module 1. Theory, seminars, and problems.
- Evaluation system: test with multiple choice answers.
- Weight in the global rating: 70%.
- Competences evaluated: CE1, CE2, CE11, CT1, CT8, CT9.
Students may opt for partial tests. There will be two partial tests throughout the semester. The first test will include unit 1 to approximately unit 12 (depending on the specific calendar). Part 2 includes unit 13 to the last unit. Each test will consist of approximately 25-30 type-test questions for each partial. Questions about seminars will be included.
1) In the case of obtaining a minimum mark of 4,5 in each partial exam, the mean of the two scores will be calculated. If the average score of the two partial exams is equal to or greater than 5, the final score will be obtained by the sum of the average of the two partials (weight 70%), the score of the practical session exam (weight 10%) and the score of self-learning activity (20% weight). If this number is equal to or higher than 5, the grade is “Pass”. If the sum is less than 5, the final grade will be “Failed”. in the case that the mark is “Failed” but the average grade of the two exams higher or equal 5, the student may retake the test to improve the mark and to pass the subject. The student will have to agree with the teachers which partial exam is to be retaken.
2) If the average of the two partial exams is less than 5, the student will have to retake the partial/partials with a score less than 5. In case that onlya partial shouldbe retaken, the grade must be equal or higher than 4.5 (out of 10). The final mark will be calculated fromthe sum of the average of the two partials (weight: 70%), the mark of the practical session exam (weight: 10%) and the mark of the self-learning activity (weight: 20%). If this number is equal to or higher than 5, the grade is Passed. If the sum is less than 5, the final grade will be Failed.
If in the retake of the partial exam the student obtains a mark less than 4.5 (out of 10), the partial exams will not compensate and therefore, the final qualification will be Failed.
3) In case the student must retake the two partial exams, the exam will be of all the subject (Module 1: theory + seminars). The exam will be corrected as a single test. The minimum mark in the recovery exam must be 4.5 (out of 10). A score lower than 4.5 represents a “Failed” as the final grade.
If the mark of the retaken exam is equal to or higher than 4,5 (out of 10), the final mark will be obtained by the sum of the retake exam (weight: 70%), the mark of the practical session exam (weight: 10%) and the mark of self-learning activity (weight: 20%). If this number is equal to or greater than 5, the final grade will be “Pass”. If the sum is less than 5, the final grade will be “Failed”.
• Module 2. Laboratory practices
Laboratory practices are mandatory. The student who has not completed them or does not present the poster will be qualified as Not Presented or Failed, depending on their situation, regardless of the score that they have obtained in the exam.
- Assessment system: design and construction of a poster about one laboratory practice (chosen by the teacher).
- Weight in the global rating: 10% (Maximum score: 1,0).
- Competences evaluated: CE1, CE2, CT1, CT2, CT8, CT9.
• Module 3. Self-learning activity
The self-learning activityis compulsory and, therefore, the student who do not takeit will be graded as “Not Presented” or “Failed”, depending on their situation and regardless of the grade that they have obtained in the exam.
- Evaluation system: work presented.
- The written and oral presentation will be evaluated, as well as the competence when discussing the topic.
- Weight in the global rating: 20% (Maximum score: 2.0).
- Skills evaluated: CE1, CE2, CE11, CT1, CT2, CT4, CT5, CT6, CT10.
Retake exam
In the retake exam, the student will be able to take the failed partial exam or both (obligatory or voluntarily) corresponding to Module 1. The obtained score, which will represent 70% of the final grade, will be added to the marks obtained in Modules 2 and 3 as indicated above.
Regardless of the score obtained in the partial tests, any student may choose to attend the retake exam to obtain a higher mark. In this case, the mark will be the one from the last exam.
Not gradable
A student is not gradable if it has participated in assessment activities that represent ≤ 15% of the final grade
Single assessment
Students who take the single assessment must do the laboratory practical sessions in the in-person sessions at the time set in the calendar. Attendance and in-person presentation of the work corresponding to Module 3 (Self-Learning activity) is also mandatory, and the student will have to attend the entire session on the indicated day. The single assessment test will coincide with the same date fixed in the calendar for the last continuous assessment test. The presentation of the poster as an evaluation system for the practices and the evaluation of module 3 will take place on the day of the single assessment.
The same non-gradable criteria as for continuous assessment will be applied. The review of the final grade follows the same procedure as for the continuous assessment.
Bibliography
Basic bibliography
- Anàlisi química quantitativa. D.C. Harris, 6 Ed. Reverté. 2006.
- Fundamentos de Química Analítica. Skoog D, West DM, Holler FJ, Crouch SR. 9 Ed. Thomson. 2014.
- Química General, Petrucci, Harwood, Herring, trad. 11 Ed. Pearson Educación. 2017.
Main texts
- Stryer L, Berg JM and Tymoczko JL. BIOQUIMICA. CURSO BASICO. 1 Ed. Reverté. 2014.
- Nelson DL, & Cox MM. Lehninger Principles of Biochemistry. 8 Ed. Freeman. 2021.
- Fennema, OR. Química de los Alimentos. 4a edición. Ed. Acribia. 2019.
- Fennema's Food Chemistry, 5th edition, 2017. By: Srinivasan Damodaran; Damodaran, Srinivasan; Kirk L. Parkin. CRC Press. https://app.knovel.com/web/toc.v/cid:kpFFCE001G/viewerType:toc/root_slug:fennemas-food-chemistry?kpromoter=federation
- Sánchez de Medina F. Tratado de Nutrición. Tomo I: Bases fisiológicas y bioquímicas de la nutrición. 3 edición. Panamericana. 2017.
Others
- Berg J, Gatto Jr G. Hines J, Tymoczko JL, Stryer L. Biochemistry. 10 Ed. Freeman & Co. 2023.
- Alberts B et al. Molecular Biology of the Cell. 7 Ed. WW Norton & Norton Company. 2022.
- Lodish H et al. Molecular Cell Biology. 9 Ed. Freeman & Co. 2021.
- Voet D, Voet JG and Pratt CW. Fundamentos de Bioquímica. 4 Ed. Panamericana. 2016.
- Champe PC and Harvey RA. Biochemistry. 3 Ed. Lippincott's Illustrated Reviews. 2004.
- Mathews C, Van Holde K, Appling D and Anthony-Cahill S. Biochemistry. 4 Ed. Adison-Wesley, 2012.
- McKee T, McKee JR. Bioquímica, las bases moleculares de la vida. 4 Ed. McGraw-Hill, 2009.
Software
- Páginas de Bioquimica y Biologia Molecular: http://biomodel.uah.es/
- Protein Purification (Dr Andrew Booth, University of Leeds, UK): http://www.agbooth.com/pp_ajax/
Language list
| Name | Group | Language | Semester | Turn |
|---|---|---|---|---|
| (PAUL) Classroom practices | 1 | Catalan | second semester | morning-mixed |
| (PAUL) Classroom practices | 2 | Catalan | second semester | morning-mixed |
| (PLAB) Practical laboratories | 1 | Catalan | second semester | afternoon |
| (PLAB) Practical laboratories | 2 | Catalan | second semester | afternoon |
| (PLAB) Practical laboratories | 3 | Catalan | second semester | afternoon |
| (PLAB) Practical laboratories | 4 | Catalan | second semester | afternoon |
| (SEM) Seminars | 1 | Catalan | second semester | morning-mixed |
| (SEM) Seminars | 2 | Catalan | second semester | morning-mixed |
| (SEM) Seminars | 3 | Catalan | second semester | morning-mixed |
| (SEM) Seminars | 4 | Catalan | second semester | morning-mixed |
| (TE) Theory | 1 | Catalan | second semester | morning-mixed |