Here, the authors devise an alternative descriptor based on hydrogen bond rotations, and apply it to describe protein structures using a vocabulary of 30 hydrogen-bonding motifs.

Hydrogen Bonds Shown To Play 'Conserved' Role In Protein Folding Date: February 13, 2006 Source: Duke University Summary: By changing individual atoms in key places in proteins, Duke University ...

Protein low-complexity domains (LCDs) stack together to form dynamic liquid droplets within the cell; alas, some pathogenic mutations in these regions encourage aggregation beyond this temporary ...

The contribution of hydrogen bonding to the thermodynamics of protein folding is not well understood. The strength of hydrogen bonds is now found to depend on the polarity of their ...

This structure makes protein-based materials as strong as steel, even though the hydrogen bonds that hold them together are 100 to 1,000 times weaker than the metallic bonds in steel.

Hydrogen bonds occur when molecules on neighboring keratin strands each form a weak attraction with the same water molecule, thereby indirectly bonding the two keratin proteins together.

Hydrogen bonding, so significant in biology, is finally being exploited as a primary adsorption mechanism. BIA Separations shows how. Its salt-tolerant approach separates proteins by size.

In protein’s beta sheets, the confined nature of the hydrogen bond clusters helps to dissipate the energy without compromising the strength of the material. This shows the amazing ingenuity and ...

Proteomics Unusual hydrogen bond plays a bigger role in proteins than chemists realized Interaction affects 94% of all proteins, study shows by Celia Henry Arnaud ...

"Who will watch the watchers?" asked Roman poet Juvenal way back in the first century C.E. Nature has been addressing that ...

The interaction of protein shell and active centre in hydrogen-producing enzymes is crucial for the efficiency of biocatalysts. A team from Ruhr-Universität Bochum and the Max Planck Institute ...

By converting their data into sounds, scientists discovered how hydrogen bonds contribute to the lightning-fast gyrations that transform a string of amino acids into a functional, folded protein.