| Code |
16890
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| Year |
1
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| Semester |
S2
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| ECTS Credits |
5
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| Workload |
TP(40H)
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| Scientific area |
BIOMEDICINA/BIOQUÍMICA/MEDICINA/CIÊNCIAS FARMACÊUTICAS
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Entry requirements |
-
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Learning outcomes |
The objective of this course is to provide students with advanced knowledge on the application of Nuclear Magnetic Resonance (NMR) spectroscopy in the structural and functional characterization of eukaryotic and prokaryotic secretomes. Students are expected to develop skills in the interpretation of spectroscopic data, identification of secreted biomolecules, and understanding the role of these molecules in biological and pathological processes. In addition, students will acquire the ability to design and implement experimental strategies based on NMR for the analysis of metabolites present in microbial and cellular secretomes.
The learning objectives will be achieved through a combination of theoretical and practical sessions focused on spectroscopic analysis, and case studies. The pedagogical approach emphasizes the integration of theoretical concepts with experimental applications, promoting students’ critical ability to interpret NMR data in complex biological systems.
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Syllabus |
The course contents are structured to ensure a logical progression from the theoretical foundations of NMR spectroscopy to its practical applications in the study of biological secretomes. The introduction to the principles of NMR provides the conceptual basis necessary for understanding the spectroscopic techniques used in the characterization of biomolecules. Subsequently, the discussion of experimental methods and sample preparation enables students to understand the key steps required for the analysis of biological systems.
The inclusion of multidimensional techniques and spectroscopic data analysis tools contributes to the development of skills in the interpretation of NMR spectra. Finally, the analysis of real examples and applications of NMR in eukaryotic and prokaryotic secretomes allows students to consolidate the acquired knowledge and develop an integrated understanding of the potential of this technique in biomedical and biotechnological research.
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Main Bibliography |
Claridge, T. D. W. (2016). High-Resolution NMR Techniques in Organic Chemistry. Elsevier.
Cavanagh, J., Fairbrother, W., Palmer, A., Rance, M., & Skelton, N. (2007). Protein NMR Spectroscopy: Principles and Practice. Academic Press.
Keeler, J. (2010). Understanding NMR Spectroscopy. Wiley.
Sattler, M., Schleucher, J., & Griesinger, C. (1999). Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution. Progress in Nuclear Magnetic Resonance Spectroscopy, 34, 93–158.
Emwas, A. H. et al. (2019). NMR spectroscopy for metabolomics research. Metabolites, 9, 123.
Markley, J. L. et al. (2017). The future of NMR-based metabolomics. Current Opinion in Biotechnology, 43, 34–40.
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Teaching Methodologies and Assessment Criteria |
The assessment of this course unit will be continuous and will aim to evaluate the acquisition of theoretical knowledge and practical skills in the application of Nuclear Magnetic Resonance (NMR) spectroscopy to the analysis of eukaryotic and prokaryotic secretomes. Assessment will include students’ active participation in theoretical and practical classes, critical analysis of relevant scientific articles in the field of NMR applied to biological systems, and exercises involving the interpretation of NMR spectra.
In addition, students will be required to prepare a short presentation or scientific report on a case study involving the use of NMR in the characterization of secreted biomolecules, including proteins, peptides, or metabolites. This assignment will allow the evaluation of the students’ ability to integrate acquired knowledge, interpret spectroscopic data, and apply NMR methodologies to current research problems.
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Language |
Portuguese. Tutorial support is available in English.
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