How hydrophobicity shapes protein assemblies

Through a nuanced balance of electrical and hydrophobic forces, biological molecules self-assemble into the large functional structures that maintain life's vital functions. Understanding how proteins self-assemble requires ...

Deep learning for new protein design

The key to understanding proteins—such as those that govern cancer, COVID-19, and other diseases—is quite simple: Identify their chemical structure and find which other proteins can bind to them. But there's a catch.

Gold adds the shine of reversible assembly to protein cages

Protein cages—capsule-like structures made up of numerous protein molecules—perform roles in nature that have inspired their application in areas such as drug delivery. Their controlled assembly is therefore of particular ...

Virus hydrophobicity can help purify vaccines

A person doesn't have to get sick to catch a virus. Researchers hope to catch viruses for detection and vaccinations by understanding their sticky outer layers.

Why do mitochondria retain their own genome?

It sounds like science fiction to suggest that every cell in the human body is occupied by a tiny genome-equipped organelle, with which we exist in symbiosis. But in actuality, eukaryotic life is dependent on mitochondria, ...

A better trigger for targeted drug delivery

Biomolecular 'nanocarriers' formed by the careful assembly of protein subunits are common in nature and perform a range of essential roles in biological processes, powered by the biological energy carrier adenosine-5'-triphosphate ...

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