Queensland's music outcomes: building pedagogical bridges

This paper discusses the challenges surrounding the implementation of the Music strand of the new syllabus for secondary teachers within the context of emerging trends in pedagogical reform in Queensland, and identifies several areas where research is needed to inform classroom music teaching practice and to guide teacher training programs. Secondary music teachers (Years 8-10) have not had the same systemic, school-based curriculum guidance that was given to teachers in years 1-7. This has resulted in a plethora of teaching and learning practices in lower secondary classrooms, many of which may be more experiential than developmental in approach and which may have little reference to the types of music programs common in primary classrooms.

Making Fedora easier to implement with Fez: A free open source content model and workflow management front-end to Fedora

The University of Queensland, Australia has developed Fez, a world-leading user-interface and management system for Fedora-based institutional repositories, which bridges the gap between a repository and users. Christiaan Kortekaas, Andrew Bennett and Keith Webster will review this open source software that gives institutions the power to create a comprehensive repository solution without the hassle..

(FAB01_091) Book reviews

Leon Battista Alberti, 'On the Art of Building in Ten Books' Translated by Joseph Rykwert, Neil Leach and Robert Tavemor L. A. Zhadova (ed.), 'Tatlin' (Budapest 1984). English translation Helen Ross, 'Just For Living, Aboriginal Perceptions of Housing in North West Australia' Tony Fry, 'Design History Australia: A Source Text in Methods and Resources' Phillip Cox and David Moore, 'The Australian Functional Tradition' Lenore Coltheart and Don Fraser (eds.), 'Lamdmarks in Public Works, Engineers and Their Works in New South Wales 1884-1914' Peter Bridges and Don MacDonald, 'James Barnet, Colonial Architect' Don Watson and Judith McKay, 'A Directory of Queensland Architects to 1940' Russell Walden, 'Voices of Silence: New Zealand's Chapel of Futuna' Jeremy Salmond, 'Old New Zealand Houses 1800-1940' Victoria Middleton, 'The Legend of Green Valley' Dyranda Prevost and Ann Rado, 'Living Places' Mark Jackson and Mark Stiles (directors), 'Universal Provider' Lars Lerup, 'Planned Assaults'

Historic Bridge Photographs: The Lahey Collection

Romeo Watkins Lahey (1887-1968) was a distinguished Queensland engineer. He graduated in engineering from the University of Sydney in 1914 and served in World War I from 1915 to 1918 with The Royal Australian Engineers. Following the war, he accepted an offer to remain for a period in England and studied town planning at the University of London. He visited Europe and collected a remarkable set of historic bridge photographs. In the course of this visit, he met Paul Sejourne, a distinguished French bridge engineer, the designer of at Ieast one of the bridges (at Fontpedrouse, pages 25-27) included in this set. When Lahey died, his wife Sybil and daughter Ann took steps to give this remarkable set of 58 historic bridge photographs to The University of Queensland. More recently, Lahey's daughters Ann Neale and Alison Drake have given a set of lantern plates collected by their father, many of which also have photographs of bridges. This volume is divided into three parts: (a) a biography of Romeo Watkins Lahey, written by his daughter, Ann Neale; (b) copies of the original set of 58 bridge photographs, and (c) copies taken from 32 lantern plates. To these have been added captions. Many of the original photographs carried titles; where these are available they have been printed in italics. Further work has been done to identify bridges and where possible the captions include the completion date, major dimensions, locations, and references to published works. Plates 8.1-10 are copies of drawings used as Figures in a book. These drawings have not been copied and the source has not been identified. Two lists of photographs and plates are included - the first in the order of the original collections and a second with bridges listed in the order of material, structural form and date. The collection is of remarkable value to any bridge historian, and is recommended for study by students.

Structural analysis and molecular model of a self-incompatibility RNase from wild tomato

Self-incompatibility RNases (S-RNases) are an allelic series of style glycoproteins associated with rejection of self-pollen in solanaceous plants. The nucleotide sequences of S-RNase alleles from several genera have been determined, but the structure of the gene products has only been described for those from Nicotiana alata. We report on the N-glycan structures and the disulfide bonding of the S-3-RNase from wild tomato (Lycopersicon peruvianum) and use this and other information to construct a model of this molecule. The S-3-RNase has a single N-glycosylation site (Asn-28) to which one of three N-glycans is attached. S-3-RNase has seven Cys residues; six are involved in disulfide linkages (Cys-16-Cys-21, Cys-46-Cys-91, and Cys-166-Cys-177), and one has a free thiol group (Cys-150). The disulfide-bonding pattern is consistent with that observed in RNase Rh, a related RNase for which radiographic-crystallographic information is available. A molecular model of the S-3-RNase shows that four of the most variable regions of the S-RNases are clustered on one surface of the molecule. This is discussed in the context of recent experiments that set out to determine the regions of the S-RNase important for recognition during the self-incompatibility response.

Calcium is essential for the structural integrity of the cysteine-rich, ligand-binding repeat of the low-density lipoprotein receptor

Seven cysteine-rich repeats form the ligand-binding region of the low-density lipoprotein (LDL) receptor. Each of these repeats is assumed to bind a calcium ion, which is needed for association of the receptor with its ligands, LDL and beta-VLDL. The effects of metal ions on the folding of the reduced N-terminal cysteine-rich repeat have been examined by using reverse-phase high-performance liquid chromatography to follow the formation of fully oxidized isomers with different disulfide connectivities. in the absence of calcium many of the 15 possible isomers formed on oxidation, whereas in its presence the predominant product at equilibrium had the native disulfide bond connectivities. Other metals were far less effective at directing disulfide bond formation: Mn2+ partly mimicked the action of Ca2+, but Ba2+, Sr2+, and Mg2+ had little effect. This metal-ion specificity was also observed in two-dimensional H-1 NMR spectral studies: only Ca2+ induced the native three-dimensional fold. The two paramagnetic ions, Gd3+ and Mn2+, and Cd2+ did not promote adoption of a well-defined structure, and the two paramagnetic ions did not displace calcium ions. The location of calcium ion binding sites in the repeat was also explored by NMR spectroscopy. The absence of chemical shift changes for the side chain proton resonances of Asp26, Asp36, and Glu37 from pH 3.9 to 6.8 in the presence of calcium ions and their proximal location in the NMR structures implicated these side chains as calcium ligands. Deuterium exchange NMR experiments also revealed a network of hydrogen bonds that stabilizes the putative calcium-binding loop.

alpha-conotoxin EpI, a novel sulfated peptide from Conus episcopatus that selectively targets neuronal nicotinic acetylcholine receptors

We have isolated and characterized ol-conotoxin EpI, a novel sulfated peptide from the venom of the molluscivorous snail, Conus episcopatus, The peptide was classified as an cy-conotoxin based on sequence, disulfide connectivity, and pharmacological target. EpI has ho mology to sequences of previously described cu-conotoxins, particularly PnIA, PnIB, and ImI, However, EpI differs from previously reported conotoxins in that it has a sulfotyrosine residue, identified by amino acid analysis and mass spectrometry, Native EpI was shown to coelute with synthetic EpI, The peptide sequence is consistent with most, but not all, recognized criteria for predicting tyrosine sulfation sites in proteins and peptides, The activities of synthetic EpI and its unsulfated analogue [Tyr(15)]EpI were similar. Both peptides caused competitive inhibition of nicotine action on bovine adrenal chromaffin cells (neuronal nicotinic ACh receptors) but had no effect on the rat phrenic nerve-diaphragm (muscle nicotinic ACh receptors), Both EpI and [Tyr(15)]EpI partly inhibited acetylcholine-evoked currents in isolated parasympathetic neurons of rat intracardiac ganglia, These results indicate that EPI and [Tyr(15)]EpI selectively inhibit alpha 3 beta 2 and alpha 3 beta 4 nicotinic acetylcholine receptors.

Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization

Background: The redox proteins that incorporate a thioredoxin fold have diverse properties and functions. The bacterial protein-folding factor DsbA is the most oxidizing of the thioredoxin family. DsbA catalyzes disulfide-bond formation during the folding of secreted proteins, The extremely oxidizing nature of DsbA has been proposed to result from either domain motion or stabilizing active-site interactions in the reduced form. In the domain motion model, hinge bending between the two domains of DsbA occurs as a result of redox-related conformational changes. Results: We have determined the crystal structures of reduced and oxidized DsbA in the same crystal form and at the same pH (5.6). The crystal structure of a lower pH form of oxidized DsbA has also been determined (pH 5.0). These new crystal structures of DsbA, and the previously determined structure of oxidized DsbA at pH 6.5, provide the foundation for analysis of structural changes that occur upon reduction of the active-site disulfide bond. Conclusions: The structures of reduced and oxidized DsbA reveal that hinge bending motions do occur between the two domains. These motions are independent of redox state, however, and therefore do not contribute to the energetic differences between the two redox states, instead, the observed domain motion is proposed to be a consequence of substrate binding. Furthermore, DsbA's highly oxidizing nature is a result of hydrogen bond, electrostatic and helix-dipole interactions that favour the thiolate over the disulfide at the active site.