The targeted engineering of artificial proteins with unique properties – that is possible with the assistance of a novel method developed by a research team of Heidelberg University. It centers around a new AI model. This allows for forecasting how two proteins have to be fitted together at the molecular level from individual parts – subunits – in order to engineer a functional, adjustable new protein.

Designing protein binders from scratch has long been a daunting challenge within the field of computational biology. Researchers have now developed an innovative, training-free pipeline that uses the fundamental principle of shape complementarity to design site-specific protein binders, which are then optimised to fit precisely onto chosen target sites. The researchers tested this on proteins linked to cancer.

A team of researchers from HITS and MPIP have developed a model that learns how to generate proteins whose structures are highly flexible, even with patterns that are uncommon in natural proteins. Their work, presented at the International Conference on Machine Learning (ICML), marks a step towards the goal of designing new proteins for applications in biotechnology, therapeutics and environmental research.

An international team of researchers led by Konstanz biologists has identified a molecular mechanism that regulates the activity of N-myristoyltransferases. This enzyme plays a role in biological signalling pathways, where dysregulation can lead to serious illness.

With the goal of creating living cells from non-living components, scientists in the field of synthetic biology work with RNA origami. This tool uses RNA biomolecule to fold new building blocks, making protein synthesis superfluous. In pursuit of the artificial cell, a research team has cleared a crucial hurdle. Using the new RNA origami technique, they succeeded in producing nanotubes that fold into cytoskeleton-like structures.

How are proteins in our cells modified while they are still being synthesized? An international team of researchers from the University of Konstanz, Caltech, and ETH Zurich has deciphered the molecular mechanism of this vital process.

The computational design of new proteins for biomedical or other applications involves long computing times on powerful servers. A joint team of researchers from the Max Planck Institute for Biology Tübingen and the University Hospital Tübingen has now developed and tested a new computational method to greatly speed up the necessary energy calculations. Their framework allows for a precise and efficient design of functional proteins.

Researchers from Konstanz and Zurich have deciphered a biochemical mechanism that ensures that newly formed proteins are processed correctly when they leave the cell's own protein factories. This solves a decade-old puzzle in protein sorting.

Mitochondria are considered to be the power plants of cells and are essential for human metabolism. Dysfunction in 40 percent of mitochondrial proteins are associated with human diseases, which is why mitochondria also play an important role in medical research. A previously unexplained process in the complex mitochondria was the formation of their barrel pores.