Biochemistry

Protein-protein interactions leading to non-physiological complexes, oligomers or aggregates are consequences of specific protein states which do not lead to thermodynamics minima of the isolated protein. These specific states - transition states are characterized by exposition of particular amino acids increasing probability to abandon normal folding pathways and end up in oligomers or aggregates.  Analogy of such process is an interaction of intrinsically disordered proteins resembling the previously described transition states paradigm. The aim of the thesis is a bioinformatic analysis of such complexes utilizing information about their structures (from structural methods or from computational models) and comparison of protein-protein interaction selectivity with globular proteins close to a thermodynamics minimum.