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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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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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