Noncovalent interactions are essential for the existence of solid and liquid phases. 1, 2
Traditionally touted as weak forces, quantification of these interactions, which govern the …

Small heat shock proteins (sHsps) are conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

Small heat shock proteins (sHsps) are a ubiquitous and ancient family of ATP-independent
molecular chaperones. A key characteristic of sHsps is that they exist in ensembles of iso …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

The small heat shock proteins (sHSPs) and the related α-crystallins (αCs) are virtually
ubiquitous proteins that are strongly induced by a variety of stresses, but that also function …

Modern classification of the family of human small heat shock proteins (the so-called HSPB)
is presented, and the structure and properties of three members of this family are analyzed …

Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has
focused on highly deuterated samples, in which only a small number of protons are …

Misfolding, aggregation, and aberrant accumulation of proteins are central components in
the progression of neurodegenerative disease. Cellular molecular chaperone systems …

Using a set of six 1H-detected triple-resonance NMR experiments, we establish a method for
sequence-specific backbone resonance assignment of magic angle spinning (MAS) nuclear …

One of the major open challenges in structural biology is to achieve effective descriptions of
disordered states of proteins. This problem is difficult because these states are …