Refine
Language
- English (3) (remove)
Has Fulltext
- yes (3)
Is part of the Bibliography
- no (3)
Keywords
- analysis (3) (remove)
Last week, this year’s ISA conference brought together over 5000 scholars and exhibitors from all over the world to discuss all things international, political, scholarly, hold meetings, get lunch together, and party at Mardi Gras (it was in New Orleans, after all!). Similar to last year, a lot of this discussing took also place on Twitter. Scholars-slash-tweeps rallied around the hashtag #isa2015 to talk to each other online about great (and not so great) panels, trends in IR scholarship, gender bias in academia, and (not surprisingly for an academic conference) coffee. Who was most active during ISA2015 on Twitter? What were the most hotly debated topics online? When did ISAlers tweet?
This paper will examine the self-reported division of housework and childcare in Germany and Poland considering the job-related spatial mobility within dual-earner couples who are living in a household together with a partner, using 2007 data from the Job Mobility and Family Lives in Europe Project. We find that men who are spatially mobile for work often report shifting housework to their partners. Polish couples show a stronger tendency toward an egalitarian division of labor than German couples do, especially in terms of childcare. But the central finding of this research is, gender trumps national differences and spatial mobility constraints. Polish and German women, whether mobile for their work or not, report doing the majority of housework and childcare compared to their partners.
Ribosomal proteins are assumed to stabilize specific RNA structures and promote compact folding of the large rRNA. The conformational dynamics of the protein between the bound and unbound state play an important role in the binding process. We have studied those dynamical changes in detail for the highly conserved complex between the ribosomal protein L11 and the GTPase region of 23S rRNA. The RNA domain is compactly folded into a well defined tertiary structure, which is further stabilized by the association with the C-terminal domain of the L11 protein (L11ctd). In addition, the N-terminal domain of L11 (L11ntd) is implicated in the binding of the natural thiazole antibiotic thiostrepton, which disrupts the elongation factor function. We have studied the conformation of the ribosomal protein and its dynamics by NMR in the unbound state, the RNA bound state and in the ternary complex with the RNA and thiostrepton. Our data reveal a rearrangement of the L11ntd, placing it closer to the RNA after binding of thiostrepton, which may prevent binding of elongation factors. We propose a model for the ternary L11–RNA–thiostrepton complex that is additionally based on interaction data and conformational information of the L11 protein. The model is consistent with earlier findings and provides an explanation for the role of L11ntd in elongation factor binding.