Biophysics

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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.