Amyloid formation has been implicated in the pathology of over 20 human diseases, but the
rational design of amyloid inhibitors is hampered by a lack of structural information about …

The structural eye lens protein γD-crystallin is a major component of cataracts, but its
conformation when aggregated is unknown. Using expressed protein ligation, we uniformly 13 C …

We describe a methodology for studying protein kinetics using a rapid-scan technology for
collecting 2D IR spectra. In conjunction with isotope labeling, 2D IR spectroscopy is able to …

The aggregation of human amylin to form amyloid contributes to islet β-cell dysfunction in
type 2 diabetes. Studies of amyloid formation have been hindered by the low structural …

Infrared spectroscopy is playing an important role in the elucidation of amyloid fiber formation,
but the coupling models that link spectra to structure are not well tested for parallel β-…

A cost-efficient, time-reducing solid-phase synthesis of the amyloidogenic, 37 residue islet
amyloid polypeptide (IAPP) is developed using two pseudoprolines (highlighted blue in …

We report a structural study on the membrane binding of ovispirin using 2D IR line shape
analysis, isotope labeling, and molecular dynamics simulations. Ovispirin is an antibiotic …

Rapid release of biopharmaceutical products enables a more efficient drug manufacturing
process. Multi-attribute methods that target several product quality attributes (PQAs) at one …

A series of non-natural infrared probes is reported that consist of a metal-tricarbonyl
modified with a −(CH 2 ) n – linker and cysteine-specific leaving group. They can be site-specifically …

The adsorption of monoclonal antibodies (mAbs) on hydrophobic surfaces is known to cause
protein aggregation and degradation. Therefore, surfactants, such as Poloxamer 188, are …