Membrane proteins constitute a significant fraction of cellular proteomes and play indispensable roles in signalling, transport, and metabolism. Their folding and subsequent stability are not only ...

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 ...

Although they are much weaker than the preeminent "covalent" chemical bonds that bind atoms in biological molecules, hydrogen bonds are known to occur at key points along the central "backbone" ...

For those outside the chemistry cognoscenti, the announcement might have seemed little more than researchers patting each other on the back. But the question of protein folding had plagued scientists ...

In living organisms, every protein—a type of biological polymer consisting of hundreds of amino acids—carries out specific functions, such as catalysis, molecule transport, or DNA repair. To perform ...

In order to fulfil their many functions, proteins must be folded into the correct shape. Researchers at the University of Basel have now discovered tiny “folding factories” in cells that enable ...

New computer simulations that model every atom of a protein as it folds into its final three-dimensional form support the existence of a recently identified type of protein misfolding. Proteins must ...

Textbooks often depict proteins in one conformation, but real life, as usual, is much messier. While some proteins have stable, unchanging structures, many others have intrinsically disordered regions ...

A team of researchers has developed a method that could transform the field of protein engineering. The new approach, called AI-informed Constraints for protein Engineering (AiCE), enables rapid and ...

A comprehensive analysis of over 500,000 human protein variants reveals that 60% of disease-causing missense mutations reduce protein stability In a recent study published in Nature, researchers used ...

A GIF showing a protein mimicking IL-2 binding to IL-2 receptors, then changing shape in response to an effector molecule, which forces it off of one of the receptors. A protein mimicking IL-2 called ...