A new LMU study shows how proteins function reliably even without a stable 3D structure – and the crucial importance not only of short sequence motifs, but also of the chemical characteristics.

The database of 200 million protein-structure predictions now includes homodimers, adding new biological relevance.

A new LMU study shows how proteins function reliably even without a stable 3D structure—and the crucial importance not only of short sequence motifs, but also of chemical characteristics.

The genomes of phages—viruses that infect bacteria—are largely composed of "dark matter": genes that encode proteins whose functions remain unknown. Less than four years ago, a team led by Prof. Rotem ...

Proteins, one of the smallest building blocks of life on Earth, hold promise for answering some of biology's biggest ...

For years, biomolecular condensates were thought to be simple, liquid-like droplets with little internal organization. New ...

In Greek mythology, Proteus, son of Poseidon and prophetic shepherd of sea-beasts, could foretell the future. The elusive sea god was difficult to capture as he assumed many forms—a lion, a serpent, ...

On Wednesday, the Nobel Committee announced that it had awarded the Nobel Prize in chemistry to researchers who pioneered major breakthroughs in computational chemistry. These include two researchers ...

AI protein function prediction uses machine learning models trained on sequence and structural data to infer protein roles at scale. Techniques such as transformer-based models enable automated ...

This Brush Up is sponsored by Quanterix. Learn more about tau biomarkers and clinical applications. Tau is a flexible protein that stabilizes the internal structure of neurons and supports ...