Full course description
Proteins are biomolecules that participate in almost all cellular functions; their structure, or lack thereof, is essential to perform them. As such, it is important to understand the principles and molecular forces that 1) dictate the acquisition of the native structure of a protein and 2) mediate the recognition between the native state of a protein and other molecules. The aim of this course is to review the molecular forces that drive a polypeptide chain to attain its native conformation starting from the unfolded state. Students will learn how mutations or even storage conditions can destabilise the native state of a protein, and hence its function. Additionally, the course will review the different mechanisms used by proteins to specifically recognise and bind to their ligands; including other proteins, nucleic acids or small organic molecules such as drugs. The course will initially provide an overview of protein structure together with the principles of thermodynamics and chemical equilibrium. Subsequently in the course, students will be introduced to different biophysical techniques commonly used to study protein folding and their interactions. Calorimetric and spectroscopic techniques will be introduced together with the basis of each technique, the information they provide, how to interpret the results and understand the benefits, limitations and complementarity of each technique.
- To introduce the students to the principles of calorimetric and spectroscopic techniques.
- To understand protein folding and its relation to function.
- To witness the function of a protein as a result of its interaction with a ligand.
- To have an overview of the biophysical techniques used to understand the kinetic and thermodynamic principles that control protein folding and binding.
- To understand how mutations can affect the native structure and function of a protein.
- CHE2003 Physical Chemistry
- CHE2006 Biochemistry
- “Proteins: Structures and molecular properties” by Thomas E. Creighton. W. H. Freeman & Co. ISBN 0-7167-1566
- “Structure and mechanism in protein science. A guide to enzyme catalysis and protein folding” by Alan R. Fersht. W. H. Freeman & Co. ISBN 0-7167-3268-8
- “Protein Folding” in Handbook of Neurochemistry and Molecular Neurobiology by A. Szilágyi, J. Kardos, S. Osváth, L. Barna and P. Závodszky. Volume 7, Chapter 10. P.p. 303-344. Springer. ISBN
- “Biophysical chemistry” in Tutorial Chemistry texts by Alan Cooper. The Royal Society of Chemistry. ISBN
- “Principles of Fluorescence Spectroscopy” by Joseph R. Lakowicz. Springer, ISBN 978-0-387-46312-4
- N.V. Sánchez Puig