Tasting the Tree of Life: Development of a Collaborative, Cross-Campus, Science Outreach Meal Event.

Communicating about science with the public can present a number of challenges, from participation to engagement to impact. In an effort to broadly communicate messages regarding biodiversity, evolution, and tree-thinking with the campus community at The College of New Jersey (TCNJ), a public, primarily undergraduate institution, we created a campus-wide, science-themed meal, "Tasting the Tree of Life: Exploring Biodiversity through Cuisine." We created nine meals that incorporated 149 species/ingredients across the Tree of Life. Each meal illustrated a scientific message communicated through interactions with undergraduate biology students, informational signs, and an interactive website. To promote tree-thinking, we reconstructed a phylogeny of all 149 ingredients. In total, 3,262 people attended the meal, and evaluations indicated that participants left with greater appreciation for the biodiversity and evolutionary relatedness of their food. A keynote lecture and a coordinated social media campaign enhanced the scientific messages, and media coverage extended the reach of this event. "Tasting the Tree of Life" highlights the potential of cuisine as a valuable science communication tool.

Shared ownership: what's the future?

The status of library consortia has evolved over time in terms of their composition and alternative negotiating models. New purchasing models may allow improved library involvement in the acquisitions process and improved methods for meeting users' future needs. Ever-increasing costs of library resources and the need to reduce expenses make it necessary to continue the exploration of library consortia for group purchases.

Mapping the ligand binding pocket in the cellular retinaldehyde binding protein.

Retinoid interactions determine the function of the cellular retinaldehyde binding protein (CRALBP) in the rod visual cycle where it serves as an 11-cis-retinol acceptor for the enzymatic isomerization of all-trans- to 11-cis-retinol and as a substrate carrier for 11-cis-retinol dehydrogenase (RDH5). Based on preliminary NMR studies suggesting retinoid interactions with Met and Trp residues, human recombinant CRALBP (rCRALBP) with altered Met or Trp were produced and analyzed for ligand interactions. The primary structures of the purified proteins were verified for mutants M208A, M222A, M225A, W165F, and W244F, then retinoid binding properties and substrate carrier functions were evaluated. All the mutant proteins bound 11-cis- and 9-cis-retinal and therefore were not grossly misfolded. Altered UV-visible spectra and lower retinoid binding affinities were observed for the mutants, supporting modified ligand interactions. Altered kinetic parameters were observed for RDH5 oxidation of 11-cis-retinol bound to rCRALBP mutants M222A, M225A, and W244F, supporting impaired substrate carrier function. Heteronuclear single quantum correlation NMR analyses confirmed localized structural changes upon photoisomerization of rCRALBP-bound 11-cis-retinal and demonstrated ligand-dependent conformational changes for residues Met-208, Met-222, Trp-165, and Trp-244. Furthermore, residues Met-208, Met-222, Met-225, and Trp-244 are within a region exhibiting high homology to the ligand binding cavity of phosphatidylinositol transfer protein. Overall the data implicate Trp-165, Met-208, Met-222, Met-225, and Trp-244 as components of the CRALBP ligand binding cavity.