The course provides students with an overview of the organisation of protein structure; primary, secondary (alpha helices and beta sheets, turns, loops, paper clips) tertiary, quaternary, the concept of motif and domains and protein function. Emphasis is given to the determination of protein structure and conformational changes by UV/VIS, Infrared, fluorescence, CD, DLS, NMR, X-ray crystallography, calorimetry, microscopy and the use of Ramanchandran plot for quantification of alpha and beta elements. The use of myoglobin and haemoglobin to illustrate the phenomenon of protein-ligand binding and in models to explain allosteric interactions and the Bohrs’ effects will also be discussed.