|Proteins normally recognize each other by their specific 3-D structure. If the key fits in the lock, a reaction can take place. However there are reactions at the onset of which the key does not really have a shape. German chemists at the Technische Universitaet Muenchen and the Max Planck Research Unit for Enzymology of Protein Folding (Halle/Saale) have now shown how this might work. Their results will appear in PNAS this week.|
Scientists led by Professor Thomas Kiefhaber (TUM) posed the question of whether local properties are sufficient for the recognition to take place or whether the unstructured binding partner first had to assume a specific spatial structure. Possible candidates were regularly structural elements such as coiled α-helices or β-pleated sheets, in which internal hydrogen bonds are formed.
In collaboration with Professor Gunter Fischer's research group at the Max Planck Research Unit for Enzymology of Protein Folding Halle/Saale, the scientists developed a novel method for observing the formation of individual hydrogen bonds in the course of a binding process.