Social policy and the changing concept of child well-being. The role of international studies and children as active participants

Social policy refers to the overall actions and services a society takes to ensure the well-being of its citizens. As such, children are at the forefront of social policy, and investing in them is both crucial for their current well-being and an investment toward the future. However, the concept of child well-being is changing. Scholars have termed this shift as one of moving from child-saving to child development or from child welfare to child well-being. This changing context, which in many ways is still developing, is complicating the effort to develop appropriate indicators and outcome measures of children\u27s quality of life and status and consequently it is complicating the evaluation of social policy and its contribution. This paper presents the changing context of children\u27s well-being, the major shifts that have occurred in the field, and their implications for evaluating social policy. It then goes on to discuss the potential of international comparisons in evaluating social policies and in particular the new role for children\u27s subjective reports on their well-being as a tool for evaluating social policy. In that regard, the paper presents the International Survey of Children\u27s Well-Being and concludes with a call for new policies that will adhere to the new concept of children\u27s well-being and serve to create a better life for children. (DIPF/Orig.

The Kirkwood Superposition Approximation, Revisited and reexamined

The Kirkwood superposition approximation (KSA) was originally suggested to obtain a closure to an integral equation for the pair correlation function. It states that the potential of mean force of say, three particles may be approximated by sum of potential of mean forces of pairs of particles. Nowadays, this approximation is widely used, explicitly or implicitly, in many fields unrelated to the problem for which it was suggested.It is argued that the KSA is neither a good approximation nor a bad approximation; it is simply not an approximation at all

Myths and verities in protein folding theories Part I: Anfinsen hypothesis and the search for the global minimum in the Gibbs energy landscape

Anfinsen’s thermodynamic hypothesis may be interpreted in two ways: One, that the native 3D structure of the protein, resides in the absolute minimum in the Gibbs energy landscape (GEL). The second, that the Gibbs energy functional, has a single (hence absolute) minimum at the equilibrium distribution of all accessible conformations of the protein. The second is equivalent to the Second Law of Thermodynamics. The first does not follow from the Second Law, and has no theoretical justification. Therefore, the search for an absolute minimum in the Gibbs energy landscape is not necessarily equivalent to a prediction of the native structure of the protein

Hydrophilic interactions; their Origin, their Magnitude and their Relevance to Protein Folding

A simple model is constructed in which the phenomenon of hydrophilic ( ) interactions may be studied exactly. This model reveals the origin of the strong interaction, as well as providing an approximate method of estimating its order of magnitude. The results are in agreement with previous theoretical calculations, as well as with experimental data, and simulated calculations. The source of the non-additivity of the interactions among three and four groups is examined. A few comments on the relevance of the interactions to the process of protein folding are discussed

Myths and verities in protein folding theories Part II: From Kauzmann’s conjecture to the dominance of the hydrophobic effect

     We start with Kauzmann’s conjecture regarding the factor which is most likely to determine the stability of the 3D structure of the proteins. We show first that Kauzmann’s model-process, on which the original conjecture was based is inadequate for the process of protein folding. The main reason for this is that protein folding involves the change in the conditional solvation of non-polar groups, not the solvation itself. The “condition†here is the presence of the protein backbone. Secondly, it is argued that various hydrophilic effects, both solvation and interactions are more likely to be dominant both in stabilizing the 3D-structure of proteins, as well as in determining the speed and the specificity of the folding process