| Código |
12486
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| Ano |
1
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| Semestre |
S2
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| Créditos ECTS |
6
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| Carga Horária |
TP(60H)
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| Área Científica |
Biotecnologia
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Learning outcomes |
This course aims to explore protein structure and conformation and their relationship with biological function, highlighting how structural alterations can lead to disease.
By the end of the course, students should be able to: identify the principles governing protein structure and folding mechanisms in vitro and in vivo; relate conformational changes to neurodegenerative diseases; explain cellular protein quality-control mechanisms; apply protein crystallization and structural analysis techniques (X-ray diffraction, circular dichroism, infrared spectroscopy, fluorescence, NMR and SPR); and critically analyse and present scientific literature.
Students will also develop key transferable skills, including scientific communication, independent learning, critical thinking, and teamwork.
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Syllabus |
1. Computational visualization and modeling of organic molecules. Analysis of protein–ligand interactions using molecular docking.
2. Physical methods for protein structure determination: X-ray crystallography and nuclear magnetic resonance (NMR); circular dichroism (CD); surface plasmon resonance (SPR) for protein–ligand interactions; infrared and fluorescence spectroscopy.
3. Structure and function of membrane proteins. Protein expression, purification, and crystallization strategies.
4. Cellular mechanisms of protein quality control.
5. Protein folding and conformational stability. Folding mechanisms in vitro and in vivo. Protein misfolding and disease: molecular mechanisms of protein aggregation in neurodegenerative disorders.
Experimental work: CD spectroscopy of proteins; amino acid structure determination by NMR; protein–ligand interaction analysis (SPR); fluorescence and IR spectroscopy of proteins; lysozyme crystallization.
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Teaching Methodologies and Assessment Criteria |
Final Grade (FG):
Module 1 (17.5%) + Module 2 (15%) + Module 3 (35%) + Module 4 (17.5%) + Seminar (15%).
Module 1: Test 1 (Crystallization).
Module 2: Individual bioinformatics assignment. Students with a grade below 9.5 must take an oral resit test, with a maximum grade of 9.5 in this module.
Module 3: Test 2 (65% NMR and SPR + 17.5% CD + 17.5% IR/Fluorescence).
Module 4: Test 3 (Protein Folding).
Seminar: Presentation and discussion of a scientific article.
Minimum grade required for course attendance: 9.5 in Module 3 and 9.5 in the Seminar.
Course approval requires course attendance and a minimum average grade of 9.5 in Modules 1, 3 and 4.
The final exam corresponds to 70% of the final grade (Modules 1, 3 and 4).
Attendance requirement (including working students): 90% of practical classes.
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Main Bibliography |
1. Mandatory
Kessel, A., Ben-Tal, N (2018) Introduction to Proteins: Structure, Function, and Motion.2nd Edition, CRC Press, Taylor and Francis Group, (ISBN 978-1-4987-4717-2)
Buxbaum, E. (2015). Fundamentals of protein structure and function (2ª ed.). Springer. DOI 10.1007/978-3-319-19920-7; ISBN 978-3-319-19919-1.
Tripathi, T., & Dubey, V. K. (Eds.). (2022). Advances in protein molecular and structural biology methods. Academic Press. ISBN 978-0-323-90264-9.
Gomes, C. M. (Ed.). (2019). Protein misfolding diseases: Methods and protocols. Humana Press. DOI 10.1007/978-1-4939-8820-4; ISBN 978-1-4939-8819-8.
-Artigos científicos selecionados.
2-Complementary
Tripathi, T., & Uversky, V. N. (Eds.). (2025). The three functional states of proteins: structured, intrinsically disordered, and phase separated. Academic Press. ISBN 978-0443218095.
Saudagar, P., & Tripathi, T. (Eds.). (2023). Protein folding dynamics and stability: Experimental and computational methods. Springer Nature. IS
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| Language |
Portuguese. Tutorial support is available in English.
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