HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein,
it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits …

Small-angle X-ray scattering (SAXS) is a biophysical method to study the overall shape and
structural transitions of biological macromolecules in solution. SAXS provides low resolution …

Most abundant in the extracellular matrix are collagens, joined by elastin that confers elastic
recoil to the lung, aorta, and skin. These fibrils are highly resistant to proteolysis but can …

Small-angle scattering of X-rays (SAXS) is an established method for the low-resolution
structural characterization of biological macromolecules in solution. The technique provides …

The proteolytic processing of collagen (collagenolysis) is critical in development and
homeostasis, but also contributes to numerous pathologies. Mammalian interstitial …

Small-angle scattering of X-rays (SAXS) is an established method to study the overall
structure and structural transitions of biological macromolecules in solution. For folded …

Collagenases of the matrix metalloproteinase (MMP) family play major roles in
morphogenesis, tissue repair, and human diseases, but how they recognize and cleave the …

Interstitial collagen mechanical and biological properties are altered by proteases that
catalyze the hydrolysis of the collagen triple-helical structure. Collagenolysis is critical in …

NMR spectroscopy is a key method for studying the structure and dynamics of (large)
multidomain proteins and complexes in solution. It plays a unique role in integrated …

Members of the matrix metalloproteinase (MMP) family have been identified as poor
prognosis markers for breast cancer patients and as drivers of many facets of the tumor …