This study establishes a standardized continuous-labeling, bottom-up hydrogen deuterium exchange mass spectrometry (HDX-MS) protocol to investigate conformational dynamics in protein–small molecule interactions, using the N-terminal domain of Hsp90 (Hsp90N) as a model system.

This study focuses on lipid droplets (LDs), which are organelles responsible for storing neutral lipids and are found across various species. The excessive accumulation of these lipids in LDs is linked to several metabolic disorders. Zebrafish, with their transparent embryos, present a valuable model for studying LD biology, though previous research has been hampered by the absence of specific LD marker proteins and limitations in purification techniques.

Adipose triacylglycerol lipase (ATGL) is a dynamic lipid droplet-associated protein involved in cellular lipolysis, which is conserved from bacteria to humans. Recent methods that measure the enzymatic activity of ATGL in vitro are established using lipid emulsions. However, the lipid emulsion platforms contain various membranous structures which reduce the accuracy of enzymatic activity determination. Therefore, a new platform and corresponding method are required for accurate measurement of ATGL enzymatic activity that represents cellular lipid and energy homeostasis. Adiposomes are artificial lipid nanostructures mimicking lipid droplets. Employing adiposome as a platform, the authors have developed an assay to measure the enzymatic activity of ATGL in vitro. Here, a detailed protocol is described to explain how to measure the activity of ATGL using adiposomes. This method successfully proves the concept of lipid droplet-mimetic lipase activity determining platform and provides a tool to identify the active sites of lipases.

A team from EPCC proposed FLAPS, a fluctuation-aware power auction strategy to optimize data center power utilization. FLAPS reduces power overload by 9%–10% while maintaining high resource utilization.