| Code |
17256
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| Year |
1
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| Semester |
S2
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| ECTS Credits |
6
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| Workload |
TP(60H)
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| Scientific area |
Biochemistry
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Entry requirements |
N.A.
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Learning outcomes |
The objectives of this curricukaunit are to convey the principles that determine the structure of macromolecules and structure–function relationships, as well as the techniques used to determine the 3D structures of biological macromolecules (X-ray , NMR, Cryo EM, and biophysical techniques for structural characterization). With this unit, students should acquire knowledge of: 1)the principles that determine the structure of macromolecules (proteins and nucleic acids); 2) the main structural classes of macromolecules and their biological implications; 3)the biological implications of structure; 4) the main techniques used to determine the 3D structure of biological macromolecules (X ray crystallography, NMR, CryoEM, and biophysical techniques for structural characterization); 5) correctly interpreting structural results and understanding structure validation criteria; 6)mastering various online computational tools as well as different molecular visualization and representation programs
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Syllabus |
Introduction to Structural Biochemistry: molecular organization and structural hierarchy.
• Chemical bonds and intermolecular forces in biological systems.
• Protein structure: structural levels, folding, and stability.
• Enzymes: structure, catalytic mechanisms, and regulation.
• Structure of nucleic acids and protein–DNA/RNA complexes.
• Structural determination methods: X-ray crystallography, NMR, cryo-EM, and biophysical techniques for structural characterization.
• Molecular dynamics and computational modeling.
• Structural alterations associated with disease.
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Main Bibliography |
11- Bibliografia de consulta/existência obrigatória
- “Introduction to Protein Structure” Branden, C.-I. & Tooze, J. Garland Pub. (1999)
- “Crystallography made Crystal Clear- A Guide for users of Macromolecular Models” G. Rhodes, 2nd Ed., Academic Press: San Diego, London (2000)
- “Biomolecular NMR Spectroscopy”, Evans, J.N.S., Oxford University Press (1995)
- Teng, Q. “Structural Biology: Practical NMR applications” Springer Science, USA (2005)
- Wüthrich, K. “NMR of Protein and Nucleic Acids”, Wiley-Interscience Pub., (1986)
- Friebolin, H. “Basic One- and Two-Dimensional NMR Spectroscopy”, VCH publishers, New York-Germany, 2ª ed. (1993)
- Determinação de estruturas tridimensionais de proteinas, Anjos L. Macedo & Brian J. Goodfellow, Quimica, 63, 1996
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Teaching Methodologies and Assessment Criteria |
2 Tests (the average of the tests must be equal to or higher than 9.5 points) or Final exam (60%)
Practical component (groups of two or three students), including carrying out a quiz and attendance in practical classes (recorded at the beginning of each class) and questionnaires (10%).
Seminar and oral presentation (15% + 15%) on a topic from the syllabus, in which students critically examine a structural model of the biological action of a given macromolecule, based on the discussion of a scientific article provided by the instructors.
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Language |
Portuguese. Tutorial support is available in English.
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