General Biochemistry
Objectives
Aims:
The aim is for students to understand the physicochemical basis of the relationship between the structure and function of biological macromolecules and the strategy of central metabolism. The teaching is organized so that students apply the theoretical concepts in the analysis of experimental results obtained in the laboratory and in solving problems.
At the end of this course, students should:
- To understand how proteins are made up and their structural organization;
- To know the techniques for purifying and characterizing proteins;
- To understand the mechanisms of oxygen transport by hemoglobin/myoglobin and distinguish between cooperative and non-cooperative binding;
- Use mathematical models to calculate the kinetic parameters of Michaelis enzymes in the absence and presence of inhibitors and the effect of temperature and pH on reactions rates;
- To know the structures of simple sugars and polysaccharides and their functions in the cell;
- To identify the constitution of nucleic acids, their physicochemical properties and their structures and functions;
- To explain the flow of genetic information from gene to protein;
- To have knowledge on the structures of the main types of lipids and their organization into biological membranes. To understand the different types of biological transport;
- Understand the flow of energy in cells and know how to quantify it, using thermodynamic functions;
- To know the central metabolic pathway, its regulation and its connection to the respiratory chain and oxidative phosphorylation.
General characterization
Code
13318
Credits
6.0
Responsible teacher
Carlos Alberto Gomes Salgueiro
Hours
Weekly - 4
Total - 56
Teaching language
Português
Prerequisites
It is recommended to review the basic concepts acquired in General Chemistry and Organic Chemistry.
Bibliography
Main bibliography:
LEHNINGER PRINCIPLES OF BIOCHEMISTRY
Nelson, D.L., & Cox, M.M.
W.H. Freeman and Company, San Francisco, 8th ed., 2021
FUNDAMENTALS OF BIOCHEMISTRY. LIFE AT THE MOLECULAR LEVEL
Voet, D., Voet, J.G. & Pratt, C.W.
John Wiley & Sons, Inc., New York, 5th ed., 2016
BIOCHEMISTRY
Berg, J.M., Tymoczko, J.L., Gatto Jr, G.J. & Stryer L.
W. H. Freeman and Company, San Francisco. 9th ed., 2022
LIPPNCOTT ILLUSTRATED REVIEWS: BIOCHEMISTRY
Ferrier, D.R.
Wolters Kluwer. 7th ed., 2017
Teaching method
Lectures (01:30, 14 weeks) and theoretical-practical lessons (03:00, 5 weeks), with the help of slides in Powerpoint; the talks are part of the teaching programme and the discussion and resolution of problems and questions are about matters of discipline. Laboratory sessions (04:00, 5 weeks) in groups of 3 to 4 students.
Evaluation method
I. General Conditions of participation, frequency and evaluation of UC
1. The UC of Biochemistry includes:
- theoretical lessons (1.5 hours per week);
- theoretical and practical classes (five sessions of 03:00)
- laboratory classes (five sessions of 04:00)
2. The participation in all laboratory classes is mandatory.
3. The evaluation process includes evaluation of the theoretical and practical parts of the curricular unit (UC).
4. Students without frequency on the practical part of the UC are excluded from the assessment of the theoretical component of the UC.
5. Extraordinary repetition sessions of laboratory work are not expected.
6. A student with frequency on the practical part but without approval in the theoretical part of the UC will retain the frequency of the practical part of the UC during for the subsequent academic years.
II. Obtaining frequency
7. The frequency of the practical part of the UC consists in the laboratory work and in its previous preparation and also in the elaboration of the respective questionnaires by each group of up to 3 students.
8. The ongoing assessment of the practical part of the UC includes:
-Capacity for the implementation of practical work in the laboratory and its appreciation by the lecturer in charge during the laboratory session.
-Assiduity and respect of the deadlines in the delivery of assignments.
-Delivery of the analysis of results and respective questionnaires.
9. The questionnaires of the practical work are responsibility of each group. The detection of plagiarism in a questionnaire, particularly on other quizzes of the UC, will result in the loss of frequency for all the members of the group.
III. Evaluation of the theoretical and practical parts of the UC
10. Ongoing evaluation of the UC consists in the execution of two tests.
11. The two theorectical tests contributes with 80% to the total grade. The remaining 20% correspond to practical test that focus on the practical work carried out in the laboratory in the current academic year (10%) and to the laboratory performance (10%).
For approval, the classification in the teorecthical component must be equal to or greater than 9.5. Previous practical grades are valid for the current year.
12. The exam does not include practical questions and keeps the percentages of 80%. The remaining 20% (practical component) correspond to the grade obtained in the practical test (10%) and in the laboratory performance (10%). For approval, the classification in this exam must be equal to or greater than 9.5.
13. The students with approval on the ongoing evaluation (tests) may improve the grade in the exam. To do so, they should follow the current regulations. Also in this case, The exam does not include practical questions and keeps the percentages of 80%. The remaining 20% (practical component) correspond to the grade obtained in the practical test and laboratory peerformance (the improvement of the practical grade is not possible).
IV. Approval and final grade
14. Only students with frequency at the UC will be assigned a final grade.
15. Students will obtain approval at the UC provided they have a final rating equal to or greater than 9.5.
Subject matter
Summary of lectures:
- Revision of key concepts (Biomolecules, Biological structures, metabolic pathways, expression and transmission of genetic information).
- The amino acids properties: peptide bonds - Classification and characteristics. Acid-base properties
- Levels of protein structure organization: primary, secondary (alpha helices, beta sheets and other structural elements), tertiary and quaternary structures. Protein isolation, purification and sequencing.
- Structure-function relationship in hemoglobin and O2 transport.
- Enzyme kinetics: Effect of pH, temperature and inhibitors.
- Biological Membranes: structure and dynamic. Biological transport: Passive-mediated transport versus active-transport.
- Metabolism (Catabolism and anabolism) and bioenergetics.
- The central catabolism: Glycolysis; lactic and alcoholic fermentation; the citric acid cycle; electron transport chain and oxidative phosphorylation.
Problem-solving sessions:
- Purification of proteins; Structure of proteins
- Structure/function relationship: myoglobin and haemoglobin– oxygen transport
- Enzyme kinetics.
- Bioenergetics and metabolism.
Laboratory sessions summary:
- Protein quantification Amino acid acid-base titrations.
- Separation of biological compounds by chromatography: A) Gel filtration; B) Ionic exchange chromatography.
- Enzymatic characterization of lactase (two sessions).
- Determination of the redox potential from cytochrome c.