Repeat proteins, defined by sequential arrays of short structural motifs, offer an intriguing departure from the folding behaviour of conventional globular proteins. Their modular architecture enables ...

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 ...

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 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 ...

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 ...

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 ...

WEST LAFAYETTE, Ind. — The shared culprit in a slew of diseases — cancers, neurodegenerative diseases, diabetes — is molecules our cells have made incorrectly. Think of them as proteins gone wrong.

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 ...