Heavier Lies Her Crown: Gendered Patterns of Leader Emotional Labor and Their Downstream Effects.

Women use power in more prosocial ways than men and they also engage in more emotional labor (i.e., self-regulate their emotions to respond and attend to the needs and emotions of other people in a way that advances organizational goals).

Assay variation confounds the diagnosis of hypovitaminosis D: a call for standardization.

Endemic hypovitaminosis D contributes to osteoporosis development. However, variation in 25-hydroxyvitamin D (25OHD) measurement is reported and confounds the diagnosis of vitamin D insufficiency/deficiency. This report emphasizes the marked variability observed in serum 25OHD measurements between laboratories.

Structural characterization of monomeric folding intermediates of recombinant human macrophage-colony stimulating factor beta (rhM-CSFbeta) by chemical trapping, chromatographic separation and mass spectrometric peptide mapping.

We have developed a strategy for the characterization of protein folding intermediates that combines selective modification of bis-cysteinyl thiol groups with melarsen oxide (MEL), chromatographic separation and mass spectrometric characterization of the resulting protein derivatives. In the unfolding reaction of recombinant human macrophage-colony stimulating-factor beta (rhM-CSFbeta) we observed monomeric M.4MEL and dimeric D.

Characterization of the folding pathway of recombinant human macrophage-colony stimulating-factor beta (rhM-CSF beta) by bis-cysteinyl modification and mass spectrometry.

Melarsen oxide [p-(4,6-diamino-1,3,5-triazin-2-yl)aminophenylarsonous acid (MEL)], which selectively bridges spatially neighboring bis-cysteinyl residues in (reduced) proteins, was used to trap folding intermediates chemically during 1) time-dependent renaturation of recombinant human macrophage colony-stimulating factor (rhM-CSF); by redox refolding in vitro; 2) reductive unfolding in the presence of the trapping reagent; and 3) denaturing unfolding reactions in urea and guanidinium hydrochloride. Characterization of intermediates from folding and unfolding reactions was performed by electrospray ionization mass spectometry (ESI-MS). In all folding and unfolding reactions a characteristic dimeric intermediate with two attached melarsen oxide (MEL) groups was observed, suggesting that these rhM-CSF beta species were important refolding intermediates.

Disulfide linkages in the in vitro refolded intermediates of recombinant human macrophage-colony-stimulating factor: analysis of the sulfhydryl alkylation of free cysteine residues by fast-atom bombardment mass spectrometry.

Fast-atom bombardment mass spectrometry was used to follow the time course of disulfide bond formation during in vitro refolding of recombinant human macrophage-colony-stimulating factor. The content of iodoacetamide-alkylated half-cystines in proteolytic peptides of trapped refolding intermediates collected at 0, 6, 17, 24, and 72 hr was determined under reducing conditions. Size-exclusion high-performance liquid chromatography analyses of the collected alkylated samples indicate that aggregated monomer proceeded through a nonaggregated monomer to an intermediate dimer and finally to the fully folded and active dimer.

Mobile domains in ribosomes revealed by proton nuclear magnetic resonance.

Ribosomes and subunits from eukaryotic and prokaryotic sources were studied by high-resolution proton magnetic-resonance spectroscopy. If all ribosomal components are firmly bound within the particle, then only broad spectra would be expected. However, relatively sharp resonances were found both in ribosomal subunits and in 70 or 80 S ribosomes.

Separation of ribosomal proteins from Escherichia coli and rabbit reticulocytes using reverse-phase high-performance liquid chromatography.

Reverse-phase high-performance liquid chromatography has been used to fractionate ribosomal proteins from Escherichia coli and rabbit reticulocytes. Different column packing materials and solvent systems were compared for their effectiveness with bacterial proteins. A large-pore (300 A) short alkyl chain support (Altex RPSC) in conjunction with a triethylamine phosphate (pH 2.