Integrative structural biochemistry

Evolution starts by the random and natural generation of point mutations in protein encoding genes. They can be silent and they can be loud and they are a natural consequence of replication in any organism where only favorable mutations are retained in the organism’s progeny. Depending on where these mutations are located in a protein’s three-dimensional structure they may lead to consequences for i.e. its folding, its activity, its intracellular interactions, its longevity in the cell and even a specific phenotype.

The function of a protein is tightly connected to its three-dimensional structure which can be determined using X-ray crystallography. In this course you will learn by doing.

You will learn how to determine a protein’s three-dimensional structure using X-ray crystallography structures from purified protein and subsequently explore how the protein’s property and function respond to point mutations.

The central focus is to understand how the detailed amino-acid interactions determine protein structural stability and binding. In this course you will be introduced to how theory, wet-labs and computing go hand-in-hand to solve real problems in protein chemistry.

In addition, application of basic chemical models and data quantification constitute a red thread throughout the teaching, and several common spectroscopic methods and experimental approaches are employed in depth.

Experimental results, progress and student conclusions will be presented/examined both in form of individual seminars and poster presentations.