Involuntary human exposure to carbamazepine: A cross-sectional study of correlates across the lifespan and dietary spectrum.

Treated wastewater (TWW) is increasingly used for agricultural irrigation, especially in arid and semi-arid regions. Carbamazepine is among the most frequently detected pharmaceuticals in TWW. Moreover, its uptake and accumulation have been demonstrated in crops irrigated with TWW.

Care at the edge of viability: medical and ethical issues.

Decision-making for extremely immature preterm infants at the margins of viability is ethically, professionally, and emotionally complicated. A standard for prenatal consultation should be developed incorporating assessment of parental decision-making preferences and styles, a communication process involving a reciprocal exchange of information, and effective strategies for decisional deliberation, guided by and consistent with parental moral framework. Professional caregivers providing perinatal consultations or end-of-life counseling for extremely preterm infants should be sensitive to these issues and be taught flexibility in counseling techniques adhering to consistent guidelines.

T-wave ion mobility-mass spectrometry: basic experimental procedures for protein complex analysis.

Ion mobility (IM) is a method that measures the time taken for an ion to travel through a pressurized cell under the influence of a weak electric field. The speed by which the ions traverse the drift region depends on their size: large ions will experience a greater number of collisions with the background inert gas (usually N(2;)) and thus travel more slowly through the IM device than those ions that comprise a smaller cross-section. In general, the time it takes for the ions to migrate though the dense gas phase separates them, according to their collision cross-section (Omega).

Analyzing large protein complexes by structural mass spectrometry.

Living cells control and regulate their biological processes through the coordinated action of a large number of proteins that assemble themselves into an array of dynamic, multi-protein complexes(1). To gain a mechanistic understanding of the various cellular processes, it is crucial to determine the structure of such protein complexes, and reveal how their structural organization dictates their function. Many aspects of multi-protein complexes are, however, difficult to characterize, due to their heterogeneous nature, asymmetric structure, and dynamics.

Metamorphic proteins mediate evolutionary transitions of structure.

The primary sequence of proteins usually dictates a single tertiary and quaternary structure. However, certain proteins undergo reversible backbone rearrangements. Such metamorphic proteins provide a means of facilitating the evolution of new folds and architectures.