The twin threshold model: risk-intermediate foraging by rufous hummingbirds, Selasphorus rufus

I developed two versions of the twin threshold model (TTM) to assess risk-sensitive foraging decisions by rufous hummingbirds. The model incorporates energy thresholds for both starvation and reproduction and assesses how three reward distributions with a common mean but different levels of variance interact with these critical thresholds to determine fitness. Fitness, a combination of survival and reproduction, is influenced by both the amount of variance in the distributions and the relative position of the common mean between the thresholds. The model predicts that risk-intermediate foraging is often the optimal policy, and that risk aversion is favoured as the common mean of the distributions approaches the starvation threshold, whereas risk preference is favoured as the common mean approaches the reproduction threshold. Tests with free-living hummingbirds supported these predictions. Hummingbirds were presented with three distributions of nectar rewards that had a common mean but Nil, Moderate or High levels of variance. Birds preferred intermediate levels of variance (Moderate) when presented with all three rewards simultaneously, and became more risk-averse as the mean of the distributions was decreased but more risk-prone as the mean was increased. Birds preferred Nil when it was paired with Moderate or with High, but preferred Moderate in the presence of Nil and High together. This reversal of preference is a violation of regularity, conventionally interpreted as irrational choice behaviour. I provide an alternative version of the TTM demonstrating that violations of regularity can occur when relative instead of absolute evaluation mechanisms are used.     

Calcium binding mode of gamma-carboxyglutamic acids in conantokins.

Conantokin-T (con-T) and conantokin-G (con-G) are two highly homologous peptide toxins found in Conus venom. The former is a 21-residue peptide with four gamma-carboxyglutamic acid (Gla) residues (at positions 3, 4, 10 and 14), while the latter is a 17-residue peptide with five gamma-carboxyglutamic acid residues (at positions 3, 4, 7, 10 and 14). Despite the apparent similarity in number and relative positions of the gamma-carboxyglutamic acid residues, (113)Cd-NMR studies indicated a distinct metal binding behavior for con-G and con-T. There appears to be four binding sites in con-G in contrast to one metal binding site in con-T. To elucidate the mode of calcium binding by the gamma-carboxyglutamic acid residues in these conantokins, we designed various analogous peptides with their gamma-carboxyglutamic acid replaced by other amino acid residues. (113)Cd-NMR experiments on conantokin analogues reveal that the major difference in the number of metal binding sites between con-G and con-T is due to the residue at position 7. We also performed molecular simulations to calculate the relative binding free energies of several potential binding sites. Based on our theoretical and experimental results, we propose a 'four-site' binding model for conantokin-G and a 'single-site' binding model for conantokin-T.     

Human endothelin converting enzyme-2 (ECE2): characterization of mRNA species and chromosomal localization.

Generation of the functionally pleiotropic members of the endothelin vasoactive peptide family is critically catalyzed by unique type II metalloproteases, termed endothelin converting enzymes (ECE). Isolation of human ECE-2 (EC 3.4.24.71) cDNAs revealed deduced open reading frames of 787 and 765 amino acids with approximately 60% identity with human ECE-1. Characterization of mRNA variants revealed mRNA structural diversity at the 5'-terminus. Two mRNA species exist containing distinct first and second exons. Furthermore, in one of these species, an in-frame deletion of the intracytoplasmic domain removed 29 amino acids. Because of the previously reported human genetic diseases ascribed to germline mutations of member genes of the endothelin family, ECE2 was localized in human chromosomes with fluorescence in situ hybridization and radiation hybrid mapping to 3q28-q29 and SHGC-20171/D3S1571, respectively.