Fundamentals of Chemistry and Biophysics
Keywords |
Classification |
Keyword |
OFICIAL |
Medicine |
Instance: 2023/2024 - 1S (of 11-09-2023 to 05-01-2024) 
Cycles of Study/Courses
Acronym |
No. of Students |
Study Plan |
Curricular Years |
Credits UCN |
Credits ECTS |
Contact hours |
Total Time |
MIM |
201 |
Official Study Plan |
1 |
- |
6 |
56 |
162 |
Teaching language
Portuguese
Objectives
1. Generally, to explain how biological molecular components, and its supramolecular organizations, work, and can be studied, based on some of the most fundamental models of Physics and of Chemistry.
2. To apply Physics models to the description of some instrumental methods of diagnostic and therapeutic, as well as to how the results from said methods may be medically used.
3. To apply Chemistry models to the description of the most important structural and reactional properties of biological carbon compounds.
4. To systematize specific knowledge about the structure of the most important biological molecules as well as how that structure relates to the biological "function".
Learning outcomes and competences
1. To understand and use basic principles of Physics that are relevant to the life sciences and specifically to the acquisition of medical data, like, for example, medical image.
2. Knowledge of the biologically important carbon compounds reactions and their mechanisms. Basic organic chemistry problem solving.
3. Structural knowledge of the most important types of biological molecules.
4. Understanding of the importance of molecular recognition, intermolecular interaction and the hydrophobic effect in biological chemistry.
5. Ability to explain the function and action mechanism of biological compounds based on its molecular structure and reactivity, namely enzymes' catalysis, kinetics and regulation.
6. Understanding of the main metabolism global organization, namely the integration of anabolism and catabolism made by NAD (and FAD) and ATP (and other NTPs).
Working method
Presencial
Program
THEORETICAL PROGRAM
A - Introduction to Organic Chemistry
1. Atomic and molecular structure: concepts and models of chemical bonding.
2. Chemistry of Biological Macroelements
2.1 Organic compounds containing Carbon and Hydrogen: saturated (alkanes and cyclo-alkanes), unsaturated (alkenes and cyclo-alkenes) and aromatic hydrocarbons. Structure and reactivity of carbon compounds. Their importance in the environment and biology.
2.2 Stereochemistry: Definition of isomerism and stereoisomerism. Biological examples. Chirality and its biological importance. Elements of symmetry. Enantiomers and diastereoisomers. Newmann, Fischer, wedge and perspective representations. Absolute configuration: the R/S system. Optical activity. Racemic mixture. Meso compounds. The D and L system in sugars and amino acids. Geometric isomerism: cis/trans and E/Z. Conformational analysis: star and eclipse confomers in alicyclic and cyclic compounds. Biological examples. Configurational stereoisomerism in cyclic compounds. Biological examples.
2.3. Organic compounds containing oxygen:
- Alcohols Ethers and Phenols: Chemical structure and physicochemical properties (hydrogen bonds). Biological examples.
- Aldehydes and ketones: Molecular orbital of the carbonyl group. Physicochemical properties. Nucleophilic addition and its importance in metabolism. Biological examples (g. photochemistry of vision).
- Carboxylic acids: Derivatives of carboxylic acid. Physical properties of carboxylic acid. Acidity of carboxylic acids. Esters synthesis: Esterification. Base-catalyzed hydrolysis of esters: Saponification. Lactones: Formation and hydrolysis. Biological examples.
2.4 Organic compounds containing nitrogen:
- Amines: Chemical structure and physicochemical properties. Basicity of amines. Heterocyclic amines. Biological examples.
- Amides and lactams: Beta lactam antibiotics - penicillins and cephalosporins. Penicillin resistance.
2.5. organic compounds containing sulfur:
- Thiols, thioethers and thiophenols. Thiols and disulfides in biochemistry.
2.6 Organic compounds containing phosphorus:
- Organic and inorganic phosphate group.
B - Biomolecules: structure and function
1. Water: Water as a biological solvent, hydrophobic effect. Water as a biological reagent.
2. Carbohydrates: Major Monosaccharides (e.g. glucose, fructose, galactose and ribose), Oligosaccharides (e.g. lactose, maltose, cellobiose and sucrose) and Polysaccharides (e.g. Starch, Glycogen and Cellulose). Glycosidic bonding. Deoxy sugars (e.g. 2-Desoxyribose). Nitroglycosylamine-containing sugars, amino sugars. Chitin and chitosan. Carbohydrates on cell surfaces.
3. Amino acids and proteins: Amino acids. Energetics of the biological synthesis of the peptide bond. Proteins, Secondary structure, Disulfide bridges between cysteine residues, Tertiary structure. Factors that interfere with protein conformation. Graphical representation of proteins and their interpretation. Quaternary Structure. Main types of biological proteins and their functions. Molecular recognition, induced complementarity. Examples of structural proteins, Examples of hormonal peptides. Examples of immunoglobulins.
4. Enzymes: Enzymatic kinetics. Complex enzyme-substrate, Transient state energetics. Examples of enzymatic mechanisms. Michaelis-Menten chemical model (MM). Kinetic equation of MM, Definition of maximum rate, Interpretation of the equation and its linearization, Interpretation of constants k2, Km and k2 / Km, Examples of kinetic constants for various enzymes. Molecular recognition in the context of enzymes.
5. Nucleic acids: ribonucleotides and deoxyribonucleotides, phosphodiester bond formation reaction. Watson-Crick bonding by hydrogen bridges between nucleotide bases, stacking of bases in water. DNA, DNA replication, RNA, Aminoacyl-tRNA synthetases, Definition of the genetic code. Ribosome, conjugated function of rRNA, mRNA and tRNA.
6. Bioenergetics: Redox cycles in the biosphere, steady state. States of carbon oxidation. Hydrolysis of ATP, ATP in the synthesis of biological bonds via nucleophilic substitution.
7. Bioelectricity: Resting condition of the axon. Action potentials. Propagation in myelinated and unmyelinated axons. Neurotransmission, chemical and electrical synapses. Electrical conduction and contraction of cardiac muscle. Pacemaker cells and Cardiomyocytes.
C - Image / Diagnosis
1. Radioactivity and radiation. Nucleus, nucleus stability and types of decay. Types of interaction of electromagnetic waves with matter with interest in medical imaging. Anatomical and functional imaging techniques. Conventional radiography. Computed Tomography (CT). Single photon emission tomography (SPECT) Positron emission tomography (PET).
2. Magnetism Introduction to Nuclear Magnetic Resonance imaging. Concept of T1 and T2 relaxation times. Concept of repetition time and echo time. Image acquisition. T1 contrast, T2 contrast and proton density imaging. Sequences of image acquisition by Nuclear Magnetic Resonance. Conventional Spin Echo sequence. Inversion recovery sequence (removal of the signal from fat or fluid). Diffusion weighted image.
3. Ultrasound and optical imaging. Ultrasound interaction with tissues. Reflection, Refraction, Attenuation. Concept of acoustic impedance. Image acquisition modes (scan types). Doppler effect. Characterization of blood flow. Colour Doppler and Spectral Doppler. Resistivity index. Arterial stenosis detected by Spetral Doppler. Optical Imaging. Penetration of light in the visible and near infrared in tissues. Fundamental notions of fluorescence. Compounds used in ophthalmology. Optical Coherence Tomography.
4.Diagnosis in neurodegenerative diseases. Alzheimer's disease and Parkinson's disease. Brief description of the associated molecular mechanisms of protein aggregation. Beta amyloid peptide, Tau proteins and alpha-synuclein. Imaging techniques used for diagnosis and monitoring.
LABORATORY PROGRAM
1. Laboratory Techniques
2. Identification of carbohydrates
3. Anthocyanin Pigments
4. DNA denaturation and spectrophotometry
5. Invertase kinetics
Mandatory literature
T.W. GRAHAM SOLOMONS and CRAIG B. FRYHLE; Organic Chemistry, 10th Edition, John Wiley & Son, Inc, 2011
José Augusto Pereira; Apontamentos de Química Biológica, ICBAS, 2014 (Freely available as eBook (PDF) in "Documents" page (FQB page, this site))
Joseph W. Kane ; Physics
Teaching methods and learning activities
Theoretical classes, presential or online, using Powerpoint presentations. Theoretical-practical classes, presential or online, of problem solving and matters related with laboratorial works. Laboratorial classes where the students work in groups of up to 3, following a written protocol.
Evaluation Type
Distributed evaluation without final exam
Assessment Components
Designation |
Weight (%) |
Exame |
100,00 |
Total: |
100,00 |
Amount of time allocated to each course unit
Designation |
Time (hours) |
Estudo autónomo |
106,00 |
Frequência das aulas |
56,00 |
Total: |
162,00 |
Eligibility for exams
Presence in at least 75% of the whole practical and laboratorial classes.
Calculation formula of final grade
Denomination of assessments (all graded at 20 points):
A1 (1st frequency taken in Intermediate Assessment 1),
A2 (2nd frequency taken in Normal season),
EN (overall exam taken in Ordinary period)
ER (overall exam taken in Appeal period).
Options for approval, Final grade, F ≥ 9.50 values:
(1) F = 0.5 x A1 + 0.5 x A2
(2) F = EN
(2) F = ER
A2 and EN assessments are simultaneous and thus mutually exclusive. It is possible to switch from option (1) to options (2) or (3) but this means permanently discarding the mark obtained in A1.
Observations
Students are not allowed to enter the classes 10 minutes after its beggining time. Adequate lab coats are mandatory in laboratorial classes.