Protein Physics

Background

Welcome to the 2009 round of the Protein Physics course! This is an advanced-level course that mostly continues where the course in molecular modeling finished, although a couple of lectures might have slight overlap.

The main aim of the course is the understanding of why/when/how amino acid polypeptides fold into protein structures, and why it is folding into exactly these structures. We will investigate what this means for the folding process, the stability of proteins, but also how it relates to e.g. evolution - are proteins more or less random sequences of amino acids, and what is the probability of a random (engineered) sequence in the lab folding to a stable protein?

To balance the theoretical chemistry/physics part of the course we will also cover cutting-edge algorithms to predict protein structure, which is quite different from reproducing the entire folding process. In fact, if your aim is merely to get a structure it is usually better to forget about the folding process! We will discuss both this and several other strange paradoxes in the course.

Although the theoretical contents is partly designed to support the parallel project course "structure prediction of globular and membrane proteins" the two courses can be taken separately. 

Finally, we will go deeper into concepts such as energy landscapes and what they mean for folding, studies of "protein" structure using simplified lattice models, modern approaches for computational de novo globular (and - brand new - now also membrane!) protein design.

Course Start

We meet on thursday january 22 at 1pm in the red lecture room in the CBR corridor at DBB on floor 4. Please contact Erik Lindahl (lindahl@cbr.su.se) if you cannot attend!

Best wishes,

Erik