Integrating Philosophy of Science Into Research on Ethical, Legal and Social Issues in the Life Sciences

This paper argues that research on normative issues in the life sciences will benefit from a tighter integration of philosophy of science. We examine research on ethical, legal and social issues in the life sciences (“ELSI”) and discuss three illustrative examples of normative issues that arise in different areas of the life sciences. These examples show that important normative questions are highly dependent on epistemic issues which so far have not been addressed sufficiently in ELSI, RRI and related areas of research. Accordingly, we argue for the integration of research on the epistemic aspects of the relevant areas of science into ELSI research to provide a better basis for addressing normative questions

Migration in an Enlarged EU: A Challenging Solution?

The 2004 and 2007 enlargements of the European Union were unprecedented in a number of economic and policy aspects. This essay provides a broad and in-depth account of the effects of the post-enlargement migration flows on the receiving as well as sending countries in three broader areas: labour markets, welfare systems, and growth and competitiveness. Our analysis of the available literature and empirical evidence shows that (i) EU enlargement had a significant impact on migration flows from new to old member states, (ii) restrictions applied in some of the countries did not stop migrants from coming but changed the composition of the immigrants, (iii) any negative effects in the labour market on wages or employment are hard to detect, (iv) post-enlargement migration contributes to growth prospects of the EU, (v) these immigrants are strongly attached to the labour market, and (vi) they are quite unlikely to be among welfare recipients. These findings point out the difficulties that restrictions on the free movement of workers bring about

Employment Protection and Parental Child Care

I examine if employment protection affects parental childcare. I find that a softer employment protection has a substantial effect on how parents use and divide paid childcare between them. The identification relies on a reform that made it easier for employers in Sweden to dismiss workers in small firms. I estimate that a softer employment protection reduces the total days of parental childcare in targeted firms, measured as total days of parental leave or temporary parental leave. Both a sorting effect and a behavioral effect can explain the reduced childcare. I also find evidence of a redistribution effect of paid parental childcare within households if only one partner was affected by the reform. I interpret the redistribution effect as a way of evading an external cost on the child

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Exploring the Aggregation Propensity of γS-Crystallin Protein Variants Using Two-Dimensional Spectroscopic Tools

The formation of amyloid fibrils is associated with many 20 serious diseases as well as diverse biological functions. Despite the importance of these aggregates, predicting the aggregation propensity of a particular sequence is a major challenge. We report a joint 2D Nuclear Magnetic Resonance (NMR) and ultraviolet (2DUV) study of fibrillization in the wild type and two aggregation-prone mutants of the eye-lens protein γS-crystallin. Simulations show that the complexity of 2DUV signals as measured by their ”approximate entropy” is a good indicator for the conformational entropy and in turn is strongly correlated with its aggregation propensity. These findings are in agreement with high-resolution NMR experiments and are corroborated for amyloid fibrils. The 2DUV technique is complementary to high-resolution structural methods and has the potential to make the evaluation of the aggregation propensity for protein variants propensity of protein structure more accessible to both theory and experiment. The approximate entropy of experimental 2DUV signals can be used for fast screening, enabling identification of variants with high fibrillization propensity for the much more time consuming NMR structural studies, potentially expediting the characterization of protein variants associated with cataract and other protein aggregation diseases