Protein footprinting with mass spectrometry is an established structural biology technique for
mapping solvent accessibility and assessing molecular-level interactions of proteins. In …

Hydroxyl radical protein footprinting (HRPF) using synchrotron X-ray radiation (XFP) and
mass spectrometry is a well-validated structural biology method that provides critical insights …

We have developed a poly (dimethylsiloxane)(PDMS) microfluidic chip to study the
directional drying of a colloidal dispersion confined in a channel. Our measurements on a …

Ancient peptides are remnants of early biochemistry that continue to play pivotal roles in
current proteins. They are simple molecules yet complex enough to exhibit independent …

The contact topology of a protein determines important aspects of the folding process. The
topological measure of contact order has been shown to be predictive of the rate of folding …

The surface hydration diffusivity of Bacillus subtilis Lipase A (BSLA) has been characterized
by low-field Overhauser dynamic nuclear polarization (ODNP) relaxometry using a series of …

Over the past decades, the TIM‐barrel fold has served as a model system for the exploration
of how changes in protein sequences affect their structural, stability, and functional …

Protein-folding can go wrong in vivo and in vitro, with significant consequences for the living
organism and the pharmaceutical industry, respectively. Here we propose a design principle …

Three-dimensional structures of proteins can provide important clues into the efficacy of
personalized treatment. We perform a structural analysis of variants within three inherited …

A vast number of therapeutic proteins are approved and available on the market. However,
there are very limited analytical approaches available for the rapid determination of primary …