Over the past decade, we have observed a massive increase in the amount of information
describing protein sequences from a variety of organisms. 1, 2 While this may reflect the …

Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …

It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

The last 15 years have seen a paradigm shift in our understanding of protein biochemistry,
with the realization that an unexpectedly high fraction of the human genome codes for …

To thrive, cells must control their own physical and chemical properties. This process is
known as cellular homeostasis. The dilute solutions traditionally favored by experimenters …

The effects of crowding in biological environments on biomolecular structure, dynamics, and
function remain not well understood. Computer simulations of atomistic models of …

There is growing interest in the development of physical methods to study the
conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In …

The interactions of clinically established anticancer Pt-based drugs with proteins play crucial
roles in Pt cellular uptake and biodistribution, as well as in determining side effects and …

For more than a century, molecular and structural biology, biochemistry, and protein
biophysics have been dominated by a “rigid” or “semi-rigid” view of a functional protein …

The notion that human α-synuclein is an intrinsically disordered monomeric protein was
recently challenged by a postulated α-helical tetramer as the physiologically relevant protein …