For many, the COVID-19 pandemic felt overwhelming and stressful due to longer work hours and caring for self and others. More people experienced anxiety, fear, anger, sadness, and helplessness. Self-care is important.
View Article and Find Full Text PDFBackground: The Longitudinal Epidemiologic Assessment of Diabetes Risk (LEADR) study uses a novel Electronic Health Record (EHR) data approach as a tool to assess the epidemiology of known and new risk factors for type 2 diabetes mellitus (T2DM) and study how prevention interventions affect progression to and onset of T2DM. We created an electronic cohort of 1.4 million patients having had at least 4 encounters with a healthcare organization for at least 24-months; were aged ≥18 years in 2010; and had no diabetes (i.
View Article and Find Full Text PDFIon mobility-mass spectrometry (IM-MS) data is interpreted as evidence that gas-phase bradykinin fragment 1-5 (BK1-5, RPPGF) [M + H](+) ions exist as three distinct structural forms, and the relative abundances of the structural forms depend on the solvent used to prepare the matrix-assisted laser desorption ionization (MALDI) samples. Samples prepared from organic rich solvents (90% methanol/10% water) yield ions having an ion mobility arrival-time distribution (ATD) that is dominated by a single peak; conversely, samples prepared using mostly aqueous solvents (10% methanol/90% water) yield an ATD composed of three distinct peaks. The BK1-5 [M + H](+) ions were also studied by gas-phase hydrogen/deuterium (H/D) exchange ion-molecule reactions and this data supports our interpretation of the IM-MS data.
View Article and Find Full Text PDFChemists are constantly striving for techniques that add dimensions of orthogonality with increased throughput and sample complexity. Ion mobility spectrometry (IM) is a gas-phase separation method that adds new dimensions to mass spectrometry (MS). IM separates gas-phase ions based on their collision cross-section and can be coupled with time-of-flight (TOF) mass spectrometry to yield a powerful tool used in the identification and characterization of proteins and peptides.
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