Protein hydrophobicity is a fundamental driver of protein folding dynamics, underpinning the formation of a central hydrophobic core that stabilises the three-dimensional structure amid an aqueous ...

In this contribution, we report studies of the nature of the dynamics and hydrophobic binding in protein-ligand complexes of human serum albumin with 2-(2'-hydroxyphenyl)-4-methyloxazole. With ...

Understanding the best ways to get a membrane protein to its destination in a cell is crucial, and the best method to make this happen is still unclear. Cell-free systems allow for interactions ...

Protein stabilization is key to tackling protein aggregation, which is involved in neurodegenerative diseases. Rajan et al. explore molecular mechanisms by which zwitterionic polymers stabilize ...

Hydration modulates aromatic interactions, explaining why Tyr is a stronger sticker than Phe in aqueous environments like protein condensates but not in the cores of folded proteins.

Proteins are most well-known for their intricate structures. The α-helices and β-sheets that form from interactions between sidechains create distinct shapes that, along with the specific amino acid ...

Amino acids that were abundant since the prebiotic era are enriched in protein binding sites of the most ancient coenzymes, supporting the plausibility of an early coenzyme–peptide world.

The formation of aggregates due to protein misfolding and resulting protein instability is associated with several diseases. Previous studies have shown the potential of sulfobetaine polymer, a ...