Allosteric regulation of protein function is a mechanism by which an event in one place of a
protein structure causes an effect at another site, much like the behavior of a …

Preparation of biological macromolecules in the pure state requires that cells be disrupted,
releasing and mixing the contents. Only the most stable and highly structured molecules can …

Intrinsically disordered proteins (IDPs) perform a broad range of functions in biology,
suggesting that the ability to design IDPs could help expand the repertoire of proteins with …

Membrane encapsulation is frequently used by the cell to sequester biomolecules and
compartmentalize their function. Cells also concentrate molecules into phase-separated …

Nucleosomes, the basic structural units of chromatin, hinder recruitment and activity of
various DNA repair proteins, necessitating modifications that enhance DNA accessibility …

Translational motion in solution, either diffusion or fluid flow, is at the heart of chemical and
biochemical reactivity. Nuclear Magnetic Resonance (NMR) provides a powerful non …

Spectroscopic studies have identified a number of proteins that appear to retain significant
residual structure under even strongly denaturing conditions. Intrinsic viscosity …

A comparison of HSQC and HMQC pulse schemes for recording 1H− 13C correlation maps
of protonated methyl groups in highly deuterated proteins is presented. It is shown that …

Proteins carry out the most difficult tasks in living cells. They do so by interacting specifically
with other molecules. This requires that they fold to a unique, globular conformation that is …

The roles of unfolded states of proteins in normal folding and in diseases involving
aggregation, as well as the prevalence and regulatory functions of intrinsically disordered …