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Full-Text Articles in Chemistry
Thermoresponsive Self-Immolative Polyglyoxylamides., Amir Rabiee Kenaree, Quinton E. A. Sirianni, Kyle Classen, Elizabeth R. Gillies
Thermoresponsive Self-Immolative Polyglyoxylamides., Amir Rabiee Kenaree, Quinton E. A. Sirianni, Kyle Classen, Elizabeth R. Gillies
Chemistry Publications
Thermoresponsive polymers with lower critical solution temperatures (LCSTs) are of significant interest for a wide range of applications from sensors to drug delivery vehicles. However, the most widely investigated LCST polymers have nondegradable backbones, limiting their applications
Formation Of Gaseous Proteins Via The Ion Evaporation Model (Iem) In Electrospray Mass Spectrometry., Elnaz Aliyari, Lars Konermann
Formation Of Gaseous Proteins Via The Ion Evaporation Model (Iem) In Electrospray Mass Spectrometry., Elnaz Aliyari, Lars Konermann
Chemistry Publications
The mechanisms whereby protein ions are released into the gas phase from charged droplets during electrospray ionization (ESI) continue to be controversial. Several pathways have been proposed. For native ESI the charged residue model (CRM) is favored; it entails the liberation of proteins via solvent evaporation to dryness. Unfolded proteins likely follow the chain ejection model (CEM), which involves the gradual expulsion of stretched-out chains from the droplet. According to the ion evaporation model (IEM) ions undergo electrostatically driven desorption from the droplet surface. The IEM is well supported for small precharged species such as Na+. However, it …
Analysis Of Temperature-Dependent H/D Exchange Mass Spectrometry Experiments., Nastaran N Tajoddin, Lars Konermann
Analysis Of Temperature-Dependent H/D Exchange Mass Spectrometry Experiments., Nastaran N Tajoddin, Lars Konermann
Chemistry Publications
H/D exchange (HDX) mass spectrometry (MS) is a widely used technique for interrogating protein structure and dynamics. Backbone HDX is mediated by opening/closing (unfolding/refolding) fluctuations. In traditional HDX-MS, proteins are incubated in D2O as a function of time at constant temperature (T). There is an urgent need to complement this traditional approach with experiments that probe proteins in a T-dependent fashion, e.g., for assessing the stability of therapeutic antibodies. A key problem with such studies is the absence of strategies for interpreting HDX-MS data in the context of T-dependent protein dynamics. Specifically, it has …