The adaptive value of sociality in mammalian groups

According to behavioural ecology theory, sociality evolves when the net benefits of close association with conspecifics exceed the costs. The nature and relative magnitude of the benefits and costs of sociality are expected to vary across species and habitats. When sociality is favoured, animals may form groups that range from small pair-bonded units to huge aggregations. The size and composition of social groups have diverse effects on morphology and behaviour, ranging from the extent of sexual dimorphism to brain size, and the structure of social relationships. This general argument implies that sociality has fitness consequences for individuals. However, for most mammalian species, especially long-lived animals like primates, there are sizable gaps in the chain of evidence that links sociality and social bonds to fitness outcomes. These gaps reflect the difficulty of quantifying the cumulative effects of behavioural interactions on fitness and the lack of information about the nature of social relationships among individuals in most taxa. Here, I review what is known about the reproductive consequences of sociality for mammals

Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein.

Desulforedoxin (Dx), isolated from the sulfate reducing bacterium Desulfovibrio gigas, is a small homodimeric (2 x 36 amino acids) protein. Each subunit contains a high-spin iron atom tetrahedrally bound to four cysteinyl sulfur atoms, a metal center similar to that found in rubredoxin (Rd) type proteins. The simplicity of the active center in Dx and the possibility of replacing the iron by other metals make this protein an attractive case for the crystallographic analysis of metal-substituted derivatives. This study extends the relevance of Dx to the bioinorganic chemistry field and is important to obtain model compounds that can mimic the four sulfur coordination of metals in biology. Metal replacement experiments were carried out by reconstituting the apoprotein with In3+, Ga3+, Cd2+, Hg2+, and Ni2+ salts. The In3+ and Ga3+ derivatives are isomorphous with the iron native protein; whereas Cd2+, Hg2+, and Ni2+ substituted Dx crystallized under different experimental conditions, yielding two additional crystal morphologies; their structures were determined by the molecular replacement method. A comparison of the three-dimensional structures for all metal derivatives shows that the overall secondary and tertiary structures are maintained, while some differences in metal coordination geometry occur, namely, bond lengths and angles of the metal with the sulfur ligands. These data are discussed in terms of the entatic state theory