Bartolino, V., Ottavi, A., Colloca, F., Ardizzone, G. D., and Stefánsson, G. 2008. Bathymetric preferences of juvenile European hake (Merluccius merluccius). – ICES Journal of Marine Science, 65: 963–969. The concept of a recruit is a basic notion in fisheries science, but it is still far from being an unequivocal term, and many diverse, even ambiguous, definitions can be found in the literature. We propose a more objective and biologically meaningful way to define the length range of recruits for species that have clear bathymetric segregation during the early stages of their life cycle. The bathymetric distribution of juvenile European hake was studied by fitting a thin plate spline to data from the national autumn trawl survey. Hake showed a stable pattern of depth preference in the 6-year dataset examined. Small hake had the greatest preference for depths of 170–220 m and appeared to move slightly deeper when they reached 10-cm total length. Larger hake persisted on the continental shelf with a preference for water 70–100 m deep, especially when they reached 18–20 cm long. The length at migration was defined as the length at which the minimum depth preference was shown, and it ranged between 13.2 and 15.8 cm depending on the year. There was a relationship between length at and depth of migration, and we provide a full description of the depth preference of juvenile hake, and test the effectiveness of the analytical approach used.

A novel approach based on molecular thermodynamics and the information theory is proposed to quantify the influence of water-miscible additives on protein stability. According to the two-state mechanism of inactivation, solvent effects are described in terms of perturbation of the equilibrium between the folded and unfolded protein forms. The model provides the dependence of the protein's melting temperature on the additive concentration. Effects of the latter are accounted for by an empirical parameter related to the free energy of transfer of the protein from the pure to the mixed solvent. The model was tested using experimental data relative to the influence of hydroxylic and aminoacidic additives on the thermal unfolding of hen egg lysozyme and erythrocyte carbonic anhydrase. Fitting parameters were correlated in terms of a theoretic information index characterizing the additive's molecule and incorporating an atomic-composition term and a topological contribution. Model calculations agreed very well with experimental data, suggesting that the molecular information content of the additive can be used effectively to correlate solvent-induced perturbations of stability. The procedure was also used to predict melting temperatures in systems containing binary mixtures of additives and to reconstruct thermal unfolding curves in the different media