A new study reveals a possible protein misfolding mechanism that may resolve a long-standing mystery of why certain proteins refold into unexpected patterns. Proteins are long molecules that must fold ...

As they are being synthesized, these nascent proteins simultaneously attempt to fold while still associated with their parent ribosome, referred to as co-translational protein folding ...

In recent years, the field of biology has been rapidly transformed by the use of deep learning technology.

A new set of artificial intelligence models could make protein sequencing even more powerful for better understanding cell biology and diseases.

In 1961 the structure of one protein, myoglobin, was known at 6 Å resolution and its 2 Å structure would soon be published. The structural determinations of hemoglobin and hen lysozyme were well ...

This kind of tight folding and packing minimizes the overall free energy of the protein. An average protein has about 300 amino acid residues. If we consider that there are twenty different amino ...

For those fuzzy on the details, here’s a progressive timeline that led to this monumental achievement. 1972: Anfinsen Presents the Protein-Folding Problem In science, it is often hard to pinpoint when ...

Shortly after AlphaGo’s success in 2016, DeepMind aimed to tackle the next challenge: protein folding. Hassabis’ and Jumper’s team won that year’s CASP, and AlphaFold1 left quite an impression for ...

A novel protein cage system can control and visualize orientational changes in aromatic side chains upon ligand binding. By inducing coordinated molecular changes, this approach enables precise ...

Proteins have four levels of structure: primary (amino acid sequence), secondary (local folding patterns like alpha helices and beta sheets), tertiary (overall 3D shape), and quaternary (assembly of ...