Studying protein interactions with expanded genetic code

Nature, using proteins composed of approximately 20 amino acids repertoire, is able to perform a large number of admirable things, many of which we are still not quite able to mimic. However, it has to be said, that the set of chemical scaffolds available to the nature is somewhat limited. Therefore, it seems plausible to assume, that we could make things better simply by introducing novel scaffolds and exploring chemical space so far unavailable. It is exactly this idea upon which expanded genetic code is based on. To set ourselves free from limitations imposed by standard genetic code. This thesis will aim to provide an overview of various attempts to this problem and will try to do so in a distinct context of studying protein interactions. I will thus try to highlight methods by which we are currently able to expand genetic code, specific chemistries and physical properties of non-canonical amino acids and biophysical methods which can profit from genetic code expansion. Keywords: expanded genetic code, non-canonical amino acid, amber codon, fluores- cence, magnetic resonance, crosslinking, click chemistr