The course is worth 15 credits and runs full time during the second half of the autumn semester.
The course aims to give insights into what type of structures proteins adopt, how three-dimensional coordinates of proteins can be determined with experimental methods and how protein structure can be modelled using computational methods.
We start by discussing the forces that drive proteins to fold into three-dimensional structures. Then we look at different approaches to characterize protein structure based on evolutionary and structural similarity and discuss modern computational methods to predict the structure of proteins based on sequence. In the second block of the course, we investigate the most important experimental methods to reveal different aspects of the structure of proteins: X-ray crystallography, neutron crystallography, cryo-electron microscopy and small-angle X-ray scattering. We describe how structural information on proteins can be used to develop better pharmaceuticals. The lectures are complemented by a variety of exercises, mostly computer-based, and a limited amount of laboratory work. The course includes site visits to Lund Protein Production Facility and MAX IV.
The course use the teaching plattform Canvas to communicate with students registered on the course.
All available course material can be found on Canvas.