Phase diagram of spin-1 bosons on one-dimensional lattices

Spinor Bose condensates loaded in optical lattices have a rich phase diagram characterized by different magnetic order. Here we apply the density matrix renormalization group to accurately determine the phase diagram for spin-1 bosons loaded on a one-dimensional lattice. The Mott lobes present an even or odd asymmetry associated to the boson filling. We show that for odd fillings the insulating phase is always in a dimerized state. The results obtained in this work are also relevant for the determination of the ground state phase diagram of the S=1 Heisenberg model with biquadratic interaction.

Functional and Structural Diversification of the Anguimorpha Lizard Venom System

Venom has only been recently discovered to be a basal trait of the Anguimorpha lizards. Consequently, very little is known about the timings of toxin recruitment events, venom protein molecular evolution, or even the relative physical diversifications of the venom system itself. A multidisciplinary approach was used to examine the evolution across the full taxonomical range of this similar to 130 million-year-old clade. Analysis of cDNA libraries revealed complex venom transcriptomes. Most notably, three new cardioactive peptide toxin types were discovered (celestoxin, cholecystokinin, and YY peptides). The latter two represent additional examples of convergent use of genes in toxic arsenals, both having previously been documented as components of frog skin defensive chemical secretions. Two other novel venom gland-overexpressed modified versions of other protein frameworks were also recovered from the libraries (epididymal secretory protein and ribonuclease). Lectin, hyaluronidase, and veficolin toxin types were sequenced for the first time from lizard venoms and shown to be homologous to the snake venom forms. In contrast, phylogenetic analyses demonstrated that the lizard natriuretic peptide toxins were recruited independently of the form in snake venoms. The de novo evolution of helokinestatin peptide toxin encoding do-mains within the lizard venom natriuretic gene was revealed to be exclusive to the helodermatid/anguid subclade. New isoforms were sequenced for cysteine-rich secretory protein, kallikrein, and phospholipase A 2 toxins. Venom gland morphological analysis revealed extensive evolutionary tinkering. Anguid glands are characterized by thin capsules and mixed glands, serous at the bottom of the lobule and mucous toward the apex. Twice, independently this arrangement was segregated into specialized serous protein-secreting glands with thick capsules with the mucous lobules now distinct (Heloderma and the Lanthanotus/Varanus clade). The results obtained highlight the importance of utilizing evolution-based search strategies for biodiscovery and emphasize the largely untapped drug design and development potential of lizard venoms. Molecular & Cellular Proteomics 9:2369-2390, 2010.

The biology and functional anatomy of Modiolarca tumida (Musculus marmoratus) Bivalvia: Mytilidae

Modiolarca tumida (Hanley, 1843) is a member of the sub-family Crenellinae (Mytilidae). The preferred habitat of the species is the test of certain ascidians. The shell is dorsally flattened, which prevents it from cutting into the test during dorso-ventral contraction of the byssal retractors. The use of the byssus enables it to surround itself completely with host tissue. Adoption of the feeding posture involves the anterior-posterior contraction of the byssal retractors, which elevates the posterior margin above the host's surface using the anterior margin as the fulcrum against the host. Modiolarca tumida are attracted by the tunicin of the host, a process probably facilitated by the host's feeding currents. The smallest individuals are found round the oral aperture. Colonization of other parts of the host may result from surface migration as M. tumida can be highly mobile, crawling by means of the very extensible foot. It is during this process that individuals may be swept away in local currents and be forced to adopt a free-living existence.

Second-order NMR spectra at high field of common organic functional groups

The proton NMR spectra of aryl n-propyl sulfides gave rise to what may appear to be first-order proton NMR spectra. Upon oxidation to the corresponding sulfone, the spectra changed appearance dramatically and were clearly second-order. A detailed analysis of these second-order spectra, in the sulfone series, provided vicinal coupling constants which indicated that these compounds had a moderate preference for the anti-conformer, reflecting the much greater size of the sulfone over the sulfide. It also emerged, from this study, that the criterion for observing large second-order effects in the proton NMR spectra of 1,2-disubstituted ethanes was that the difference in vicinal coupling constants must be large and the difference in geminal coupling constants must be small. n-Propyl triphenylphosphonium bromide and 2-trimethylsilylethanesulfonyl chloride, and derivatives thereof, also exhibited second-order spectra, again due to the bulky substituents. Since these spectra are second-order due to magnetic nonequivalence of the nuclei in question, not chemical shifts, the proton spectra are perpetually second-order and can never be rendered first-order by using higher field NMR spectrometers.