Eco-evolutionary origins and diversification in a megadiverse hotspot: Arthropods in the Greater Cape Floristic Region.

The Greater Cape Floristic Region at the southern tip of Africa is a global megadiversity hotspot. The region's biodiversity has been driven by a long history of topographic, climatic, and sea level change coupled with geological uplift, and without being exposed to any major climate events such as glaciations since the breakup of Gondwana. Among arthropods, this long history has led to the survival of many ancient lineages, manifested by much disparity followed by considerable speciation in more recent times, with the emergence of many cryptic species flocks.

Condition-dependent survival and movement behavior in an endangered endemic damselfly.

Movement is essential for the maintenance of populations in their natural habitats, particularly for threatened species living in fluctuating environments. Empirical evidence suggests that the probability and distance of movement in territorial species are context-dependent, often depending on population density and sex. Here, we investigate the movement behavior of the spring cohort of an endangered endemic damselfly Calopteryx exul in a lotic habitat of Northeast Algeria using capture-mark-recapture (CMR) of adults.

Enhanced Grand Canonical Sampling of Occluded Water Sites Using Nonequilibrium Candidate Monte Carlo.

Water molecules play a key role in many biomolecular systems, particularly when bound at protein-ligand interfaces. However, molecular simulation studies on such systems are hampered by the relatively long time scales over which water exchange between a protein and solvent takes place. Grand canonical Monte Carlo (GCMC) is a simulation technique that avoids this issue by attempting the insertion and deletion of water molecules within a given structure.

Water Networks in Complexes between Proteins and FDA-Approved Drugs.

Water molecules at protein-ligand interfaces are often of significant pharmaceutical interest, owing in part to the entropy which can be released upon the displacement of an ordered water by a therapeutic compound. Protein structures may not, however, completely resolve all critical bound water molecules, or there may be no experimental data available. As such, predicting the location of water molecules in the absence of a crystal structure is important in the context of rational drug design.