Scientists have developed an artificial metalloenzyme that catalyses a reaction inside of cells without equivalent in nature. This could be a prime example for creating new non-natural metabolic pathways inside living cells.
Proteins fulfill vital functions in our body. They transport substances, combat pathogens, and function as catalysts. In order for these processes to function reliably, proteins must adopt a defined three-dimensional structure. Molecular 'folding assistants', called chaperones, aid and scrutinize these structuring processes. Researchers have now revealed how chaperones identify particularly harmful errors in this structuring process.
Scientists have successfully shown how the ultrafast processes by which proteins do their work can be studied with free-electron X-ray lasers. As a model organism, they used a simple microbe that can convert light into chemical energy.
The cell's internal skeleton undergoes constant restructuring. Physicists show that its associated proteins can be efficiently transported to their sites of action by diffusion - provided they can be arrested when they get there.