Thioredoxins are small globular proteins that proved to be excellent model for investigating the relationship between the structure of protein and their physico-chemical and functional properties. The results from the experiments on thioredoxins offer the basic for the development of the new paradigms in the field of chemistry, biophysics and biology of proteins, with special attention to redox...

Background: Septins are members of highly conserved polymerizing GTP binding proteins well described in the animal kingdom. 14 Septin proteins have been characterized in humans (SEPT1-SEPT14), some of which are tissue-specific. All of 14 genome-mapped human septins contain a highly conserved central GTP-binding domain which is very critical in GTPase signaling properties as well as oligomerizat...

Protein-protein interactions (PPIs) are involved in many cellular processes. Experimentally obtained protein quaternary structures provide the location of protein-protein interfaces, the surface region of a given protein that interacts with another. These regions are termed half-interfaces (HIs). Canonical HIs cover roughly one third of a protein's surface and were found to have more hydrophobi...

We develop and test a new hierarchical approach for the prediction of protein structure. An algorithm is described to assemble the 3D fold of a protein starting from its secondary structure and β-sheet topology. Reconstruction is carried out by energy minimization of a reduced protein model, where β-partners are derived from appropriate distance constraints imposed by the knowledge of βsheet mo...