Universitat Internacional de Catalunya
Biochemistry I
Other languages of instruction: Catalan, English
Teaching staff
The doubts related to the subject will be solved with the assigned instructor. Please ask for an appointment by e-mail.
Instructors:
- Dr. Jorge Pérez-Valle (coordination, CMs and MCs); jperezv@uic.es
- Dra. Veronica Venturi (CMs and MCs); vventuri@uic.es
- Dr. Miguel Baena (CMs and MCs); mbaena@uic.es
- Lídia Romero (Lab. practices); lromerocor@uic.es
Introduction
Biochemistry I is a 6-ECTS basic subject of the first semester from Biomedicine studies. This subject further the students' knowledge on Organic Chemistry and Macromolecules Biochemistry acquired along their high school diploma. The basic topics of the subject are related to general concepts about the structure and function of the biological molecules. Therefore, the subject aims to explain the processes related to the structure of the most abundant organic molecules and their relationship with the function in the organism.
Pre-course requirements
Prerequisites are not required
Objectives
The general objective of the subject is to provide the foundations of biochemistry that are considered necessary for the understanding of different subjects of the Degree in Biomedical Sciences.
Competences/Learning outcomes of the degree programme
- Apply the principles of organic chemistry and biochemistry in the study of the structure and function of biomolecules and their metabolism.
- Recognize the basic biological concepts and the proper language of the biomedical sciences in the state of health.
- Develop the capacity of organization and planning appropriate to the moment.
- Interpret experimental results and identify consistent and inconsistent elements.
- Know how to communicate, make presentations and write scientific papers.
- Be able to carry out autonomous learning
- Apply theoretical knowledge to practice
- That students have demonstrated to possess and understand knowledge in an area of study that starts from the base of general secondary education, and is usually found at a level that, although supported by advanced textbooks, also includes some aspects that imply knowledge coming from the forefront of his field of study
- That students have the ability to gather and interpret relevant data (usually within their area of study) to make judgments that include a reflection on relevant social, scientific or ethical issues.
- That students can transmit information, ideas, problems and solutions to a specialized and non-specialized public
Learning outcomes of the subject
At the end of the course, the student:
- Know the structure and function of biomolecules.
- Applies the principles of organic and inorganic chemistry in the study of biomolecules and fundamental biochemical processes and comprises the basic chemical formulation.
- Know the biochemical and molecular bases of folding, intracellular trafficking, post-translational modification and protein turnover.
- Solve exercises and problems raised during the course
- Can find the necessary information to complete the tasks of the subject and synthesize it.
Syllabus
UNIT I: THE CHEMISTRY OF LIFE
Topic 1. Introduction to Organic Chemistry. Introduction to the chemical bond. Covalent bond and Lewis structures. Resonance. Molecular geometry Simple and multiple carbon bonds Kinetic and thermodynamic stability of carbonated chains.
Topic 2. Organic reactions in biological systems Introduction to organic reactions. Classification of organic reactions. Oxidation and reduction reactions.
Topic 3. Thermodynamics and equilibrium. Chemical thermodynamics Energy, heat and work. Entropy and second law of thermodynamics. Process management Free energy. Chemical potential Free energy and chemical reactions: chemical equilibrium. Changes of free energy and constant balance. High energy phosphate compounds: energy sources of biological systems. Potential for phosphate transfer.
Topic 4. Composition of living matter. Water and shock absorber systems. Constitution of living beings. Structure, characteristics and properties of water. Biological importance Distribution in the human organism. Water as a solvent Acids and bases: proton donors and acceptors. Ionization of water and ionic product. PH concept. PH scale and physiological values. Balances of acids and weak bases. pKa and factors that affect the dissociation of acids. Buffer solutions of biological importance. Functioning. Types: bicarbonate buffer, phosphate buffer, ammonium buffer. Metabolic and respiratory alterations of the acid-base balance. Molecules with multiple ionizable groups: ampholytes, polyanfolites, polyelectrolytes.
Topic 5. Weak interactions in aqueous media. Nature of non-covalent interactions. Load-load interactions. Permanent and induced dipoles. Van der Waals radio. Links of H.
UNIT II: CARBOHYDRATES
Topic 6. Structure and function of carbohydrates. General characteristics and classification. Monosaccharides: structure, properties, derivatives and biological interest. Aldosas, ketoses. Enantiomeros Ring structures. Disaccharides. The glycosidic bond. Relevant disaccharides in human nutrition. Oligosaccharides. Structure, properties and biological interest. Reserve and structural polysaccharides. Glycogen, starch and cellulose. Glycoproteins Proteoglycans, glycosaminoglycans and associated pathologies. Glycoproteins with N and O bonds. Blood group antigens. Oligosaccharides as cell markers.
Topic 7. Nutritional requirements of carbohydrates. Digestion. Glucose content in foods. Glycemic index.
UNIT III: PROTEINS
Unit 8. Structure and function of proteins. Structure and properties of amino acids (structure, stereochemistry, properties). Peptides and peptide bond. Levels of protein structuring. Primary, secondary, tertiary and quaternary structures. Description of molecular helices and folded sheets. Factors that determine the secondary and tertiary structures.
Topic 9. Protein nutritional requirements. Digestion. Foods rich in proteins. Vegetable protein vs. animal protein
Item 10. Fibrous and globular proteins. Fibrous: keratins, fibroins, collagen, elastin. Globular: folding patterns, tertiary structure and functional diversity. Structure and function Transport and storage of oxygen: functions of hemoglobin and myoglobin. Hemoproteins. Variability of the protein structure: the case of immunoglobulins.
Topic 11. contractile systems and molecular motors. Actin system - myosin. Structure of the muscle and contraction mechanism. Role of calcium. Non-muscular actin and myosin. Microtubules for mobility. Movements of cilia and flagella.
Topic 12. Enzymes and enzymatic kinetics. Enzymatic regulation. Nature, nomenclature and classification of enzymes. Introduction to enzymatic catalysis: activation energy. Active site and substrate binding models. Catalytic reactions. Holoenzyme and apoenzyme. Prostetic group and coenzymes. Cofactors: metalloproteins. Michaelis-Menten model. Km and Vmax. kcat. pH, temperature and ionic strength roles on enzymatic activity. Isoenzymes.
Topic 13. Enzymatic regulation. Irreversible regulation: zymogens. Reversible regulation: phosphorylation, acetylation. Cooperativity and alosterism. Enzymatic inhibition: reversible and irreversible.
UNIT IV: LIPIDS
Topic 14. Lipids. General characteristics of lipids. Types of lipids and functions. Physicochemical properties and nomenclature. Fatty acids. Triacylglycerols Soaps and detergents. Waxes
Topic 15. Nutritional requirements of lipids. Lipid digestion. Lipid content in foods. Trans fat. Use of lipids in the industry.
Topic 16. Biological membranes composition, fluidity, asymmetry. Membrane proteins. Structure and function of lipoproteins and intracellular lipid bodies. Movement and asymmetry of the membrane. Plasma membrane and nuclear membrane. Liposomes and micelles
UNIT V: NITROGENATED COMPOUNDS AND NUCLEIC ACIDS.
Topic 17. Nucleic acids. Types of nucleotids. Composition and function of the DNA and RNA. The central dogma of biology. DNA replication, transcription and translation. Genetic code.
Topic 18. Utilization of nitrogen. Use of inorganic nitrogen. N ammonia cycle. Toxic deactivation and excretion of ammonia.
Topic 19. Vitamins. Water soluble vs fat soluble. Composition and functions. Presence in foods and related pathologies.
Topic 20. Oxidative stress. What it is, where it comes from and how it affects us. Examples of related pathologies.
Teaching and learning activities
In person
Lecture (Master class, CM): Explanation of a theoretical topic by the instructor, during 1:30h.
Case Methods or clinical cases (MC): Approach of a real or imaginary situation. Students work on the problem in small groups and later in class the answers are discussed. The instructor actively participates and, if necessary, explain new knowledge to the students.
Practical (P):Experimental demonstration in the laboratory about concepts studied in theoretical classes. Familiarization with the most frequent experimental techniques used at a biochemistry laboratory.
Virtual Education (EV): Online material that the student can consult from any computer, at any time and that will contribute to self-learning concepts related to the subject
Evaluation systems and criteria
In person
Students in first and second call:
The average grade will be calculated taking into account the different evaluable activities that will be carried out throughout the course:
- Midterm exam 20%
- Lab lessons exam 10%
- Final exam 60%
- Clinical cases or case methods 10%
The subject will be approved when the total sum-up of the parts is equal or above 5.
To be considered:
1) In the final exam, a minimum grade of 5 must be obtained in order to be able to average the marks of continuous evaluation (case, attitude and partial methods).
2) Examinations will be in multiple choice format with 4 options of answer, counting +1 the correct answer and -0.33 for each error.
3) 10% of the examination questions may cover concepts not explained in the classroom but contained in the recommended reading.
4) Participation in class means the contribution of interesting ideas or the presentation of pertinent questions that help to improve the quality of the session, whether master's lesson or clinical case, as well as using the camera during the lessons in the digital teaching. Those students who are actively involved in the course will have the option to have an extra 10% of excellence.
5) Attendance:
- Regular attendance to lectures and case methods is recommended. Lecture’s attendance is not mandatory, but students will have to follow the standards indicated by the instructors.
- Attendance to clinical cases (MC) and practical lessons is mandatory and students must attend in the assigned groups.
- The expulsion of student from lectures or case methods will have a negative impact on the evaluations. The expulsion of a student from the laboratory classroom will mean the automatic fail of the subject.
Students repeating the subject:
Lab lessons and MC grades will be keep in their profiles, although whenever they wish, students will be able to repeat class attendance and obtain a new grade. If it is his/her wish, the studend could sit for the midterm exam, or directly go to the final examination.
Bibliography and resources
Chang, Raymond. Química. 11ª ed. McGraw-Hill, 2013.
Lehninger. Principios de Bioquímica. 4ª ed. Nelson D. y Cox, M. Editorial Omega, 2005.
Stryer, Berg y Tymoczko. Bioquímica. 5ª ed. Ed. Reverté, 2002.
C.K. Mathews, K.E. Van Holde y K.G. Ahern (2002) Bioquímica. 3ª Edición. Pearson Educación.
Evaluation period
- E1 13/01/2023 A16 14:00h
- E2 21/06/2023 A15 18:00h