Laboratory of Protein Dínamics Researchgroup

An ongoing, rapid transition is taking place in molecular biology. In the last 50 years this field was guided by two central dogmas. The first linked the biological function of the protein to its unique three-dimensional structure. The second assumed that specific interactions of proteins are unambiguous. A series of ample experimental evidence demonstrates however, that these concepts need to be revisited. A ‘new view’ is being developed, where conformational diversity of proteins is recognized and furthermore, is required for a variety of functions1. Structural heterogeneity ranges from changes in side-chain conformations to alternative packing of the whole protein chain 2. Pertinent examples are the intrinsically disordered (ID) proteins, which do not adopt a well-defined three-dimensional structure, but may possess transiently structured elements3,4. The discovery of ID proteins caused an earthquake in structural biology and opened novel perspectives. Probably the most exiting one is how conformational heterogeneity promotes multiple functions of the same protein and how these functions can be modulated5.