Coil conversion to [beta]-strand induced by dimerisation

Proteins are responsible for a large number of varied functions within organisms. Such functions include catalysing metabolic reactions, DNA replications or transporting other molecules within and/or outside the cell. That variety of functions implies a diversity of shapes and structures amongst proteins. hence, a protein's environment can vary and may also affect its secondary structure. In this study, the focus is on proteins interacting together. More precisely, homodimers with [beta]-sheet interfaces. The investigation is centred on the discovery and analysis of [beta]-sheet interfaces resulting from the conversion of coil sequences into [beta]-strands, named 'dimorphics' interfaces. All homodimers in the Protein Data Bank relying on those dimorphics sequences have been identified. Initial analysis based on sequential and functional features has revealed that many of those dimers display specific properties which could contribute to their detection. Such result is important since it could provide some insight on dimerisation mechanisms.