1- Know the structure of biomolecules.   

2- Establish relationships between structure and function of biomolecules.    

3- Understand the behavior of biomolecules in biological media.    

4- Know and know how to use the basic concepts of enzymology and the regulation of enzymatic activity.

COMPETENCES

The curriculum is methodologically organized so that students in addition to

acquire knowledge and that they know how to apply it, they must acquire competences and

professionals. Starting from this idea and in accordance with the MINISTERIAL ORDER

ECI / 332/2008, the training of graduates at the Lleida School of Medicine

will guarantee that the interested party has acquired the necessary knowledge to exercise the

following competencies:

General competences

PROFESSIONAL VALUES, ATTITUDES AND BEHAVIORS

 SCIENTIFIC FOUNDATIONS OF MEDICINE:

CG 7. Understand and recognize the normal structure and function of the human body, at the

molecular, cellular, tissue, organic and systems, in the different stages of life.

CG 8. Recognize the bases of normal human behavior and its alterations.

GC 9. Understand and recognize the effects, mechanisms and manifestations of the disease

on the structure and function of the human body.

CG 10. Understand and recognize the causative agents and risk factors that determine

the states of health and the development of the disease.

CG 11. Understand and recognize the effects of growth, development and

aging on the individual and his social environment.

CG 12. Understand the foundations of action, indications and efficacy of interventions

based on available scientific evidence.

INFORMATION MANAGEMENT:

CG 30. Know, critically assess and know how to use the sources of clinical information and

biomedical to obtain, organize, interpret and communicate scientific information and

sanitary.

CG 31. Knowing how to use information and communication technologies in activities

clinical, therapeutic, preventive and research.

CG 32. Maintain and use records with patient information for later

analysis, preserving the confidentiality of the data.

CRITICAL ANALYSIS AND INVESTIGATION:

CG 33. Having, in professional activity, a critical, creative point of view, with

constructive and research-oriented skepticism.

CG 34. Understand the importance and limitations of scientific thought in the

study, prevention and management of diseases.

CG 35. Be able to formulate hypotheses, collect and critically assess information

for problem solving, following the scientific method.

CG 36. Acquire basic training for research activity.

UNIT 1. Molecular organization in living beings. Chemical characteristics differentiates from living matter. Levels of molecular organzation in living beings: Bioelements. Biomolecules.

UNIT 2. Water and ions in aqueous solution. Biological importance of water. Water structure and physical-chemical properties. Interaction of water molecules with each other, and with other biological componenets. Ionic composition of  body medias. Acid-base balance. Buffer systems

UNIT 3. General principles of organic chemistry. Links between carbons. Carbonate skeletons Links with heteroatoms. Hydrocarbons. Concept of functional group. Stereochemistry. Fischer projection. Isomerism and types.

UNIT 4. Functional groups and classes of organic compounds. Functional groups with simple bonds: structure and characteristics of alcohols, ethers, peroxides, amines, thiols, thioethers, dithiols. Functional groups with multiple bonds: structure and characteristics of aldehydes, ketones, carboxylic acids, esters, amides, IMIDA, imines.

UNIT 5. Heterocycles. Heterocycles with a heteroatom in the skeleton of the cycle: pyrrole, furan, pyridine pyrano and derivatives. Heterocycles of more complex structure, quinoline, indole and derivatives. Heterocycles with more than one heteroatom: imidazole and derivatives, pyrimidine and pyrimidine bases, purine and purine bases. Nucleoside nucleotides.

UNIT 6. Carbohydrates. Generalities Classification. Monosaccharides: aldoses and ketoses. Stereochemistry of monosaccharides. Reactivity of monosaccharides. Derived monosaccharides. Oligosaccharides: the glycosidic bond. Nomenclature structure and properties of disaccharides. Polysaccharides: characteristics of structural, reserve and gelling polysaccharides. Glycosaminoglycans. Proteoglycans Glycoproteins

UNIT 7. Lipids. General characteristics and classification. Fatty acids. Acylglycerides. Glycerophospholipids. Sphingolipids: sphingophospholipids and sphingoglycolipids. Prostaglandins. Leukotrienes. Thromboxanes Isoprenoid lipids: terpenoids, carotenoids and steroids (sterols, acids and bile salts, steroid hormones). Pyrrolic lipids.

UNIT 8. Amino acids, peptides and proteins. Amino acids protein components. Structure and properties of amino acids. Rare and non-protein amino acids. Peptide bond. Peptides Proteins Primary, secondary, tertiary and quaternary structure of proteins. Folding of proteins. Structure-function relationship in proteins, examples. Structural characterization and physical-chemical properties of proteins.

UNIT 9. Biocatalysis. Molecular structure of enzymes. Mechanism of enzymatic reactions. General characteristics, active center, catalytic center and union center. specificity of enzymes. main classes of enzymes. Structural characteristics. Isozymes. Effect of the enzymes on the speed and on the equilibrium constant of the catalyzed reaction. Activation energy concept.

UNIT 10. Kinetics and regulation of enzymatic activity. Control of enzymatic activity. Influence on the speed of the enzymatic reactions of the pH, the ionic strength and the temperature. Enzymatic reactions with a single substrate and with several substrates. Kinetic constants Vmax, Kcat, Km. And S0.5. Alosterism Mechanism of activation of proenzyme (zymogens).

UNIT 11. Vitamins. Vitamins as cofactors, precursors of cofactors, or prosthetic groups of certain enzymes. Describe and explain the structure, function, activation process, places and mode of action of vitamins

PRACTICAL AGENDA: Seminar 1. Buffer systems. (2h) Seminar 2. Spectrophotometry. Endpoint and kinetic studies. (2h) Seminar 3. Chromatographic techniques. (2h) Problems 1. Enzymatic kinetics. (2h)

LABORATORY PRACTICES

Practice 1. Espectrophotometry (2h)

Practice 2. Determination of the concentration of serum protein. (2h)

Practice 3. Electroforesi. Proteynogram (3h)

Practice 4. Enzymatic kinetics. Assay of the activity of the enzyme alfa amylase. Kinetic constants calculation (3h)

DIRECTED ACTIVITY: Bibliographic works. Preparation and exhibition of the works (5h)

TEO: teoria

PRO: Problemes i casos

SEM: Seminari

INF: Informàtica

CAM: Camp

VIS: Visites

ACD: Activitat dirigida                 

LAB: pràctiques laboratori

AVA: avaluació                                                           

S: setmana d’exàmens

- Theoretical classes: 100 presential. 

- Seminars: Eithe presentials or  virtuals  (Connection through the "videoconference" tab). Previously, the ppt that will be passed in class will have been attached in "resources". Students can print it out and follow the class better.

-Computer seminars:ppresentials

-Practices: presentials

- Exams: All face-to-face.

From 4 in exams 1 and 2, it will be averaged with the notes of the written tests of seminars and practices and work. If the result is 5 or more, the corresponding part of the subject is approved and it is not necessary to make up. If the exam grade is less than 4 or the average with the other tests is less than 5, the corresponding subject must be recovered.

1. Baynes JW, Dominiczak MH. 2011. Bioquímica Médica. 3ª edición. Ed. Elsevier

2. Branden C, Tooze J. 1999. Introduction to protein structure. 2n edition. Garland Publishing

3. Champe PC, Harvey RA, Ferrier DR. 2005. Bioquímica. 3a edición. Ed. Mc Graw-Hill Interamericana

4. Devlin TM. 2010. Texbook of Biochemistry with Clinical Correlations. 7th edition. Wiley-Liss Ed.

5. Ferrier DR. 2013. Biochemistry. Lippincott’s Illustrated Reviews. 6th ed. McGraw-Hill

6. Mathews CK, et al. 2013. Bioquímica. 4ª edición. McGraw-Hill Interamericana.

7. Rodwell VW, et al. 2015. Harper’s Illustrated Biochemistry. 30th ed. Ed. John Wiley– Sons.

9. Nelson DL, Cox MM. 2014. Lehninger. Principios de Bioquímica. 5ª ed. Ed. Omega.

10. Scriver CR, et al. 2001. The Metabolic & Molecular Basis of Inherited Disease. 8th Ed. McGraw-Hill. 4 vol.

11. Strayer L, Berg J, Tymoczko J. 2014. Bioquímica. 7ª ed. Ed. Reverté ( 6ª edició en català).

12. Strayer L, Berg J, Tymoczko J. 2014. Bioquímica. Curso básico. Ed. Reverté.

13. Voet D, Voet JG, Prat CW. 2016. Fundamentos de Bioquímica. 4a ed. Editorial Médica Panamericana

14. Vargas A 2020. Bioquimica Estructural y Biologia Molecular. Editorial Fleming.