White stem borer damage and grain yield in irrigated rice in West Java, Indonesia

Factors influencing the relationship between whiteheads caused by the white stem borer Scirpophaga innotata (Walker) and grain yield were investigated. We determined the effect of different numbers of whiteheads on grain yield using different cultivars, nitrogen application, and at different field locations in Cilamaya, West Java. At the same number of panicles and whiteheads per plant, yield reduction is greater in cisadane than in IR64. With increasing nitrogen application, the range in panicle height increased. Except for Ketan, more whiteheads were recorded in shorter panicles. Two locations planted to the same cultivar showed different relationships between whiteheads and grain yield. The relationship between whiteheads and grain yield depends on the distribution of whiteheads in the field. Unless these factors have been taken into consideration, it may be difficult to make a damage prediction of white stem borer in the field. (C) 1997 Published by Elsevier Science Ltd.

Modelling basin level allocation of water in the Murray-Darling Basin in a world of uncertainty, Murray-Darling Program Working Papers WPM05-1, Risk and Sustainable Management Group, 8 February 2005

Abstract: The Murray-Darling Basin comprises over 1 million km2; it lies within four states and one territory; and over 12, 800 GL of irrigation water is used to produce over 40% of the nation's gross value of agricultural production. This production is used by a diverse collection of some-times mutually exclusive commodities (e.g. pasture; stone fruit; grapes; cotton and field crops). The supply of water for irrigation is subject to climatic and policy uncertainty. Variable inflows mean that water property rights do not provide a guaranteed supply. With increasing public scrutiny and environmental issues facing irrigators, greater pressure is being placed on this finite resource. The uncertainty of the water supply, water quality (salinity), combined with where water is utilised, while attempting to maximising return for investment makes for an interesting research field. The utilisation and comparison of a GAMS and Excel based modelling approach has been used to ask: where should we allocate water?; amongst what commodities?; and how does this affect both the quantity of water and the quality of water along the Murray-Darling river system?

NMR structure and backbone dynamics of a concatemer of epidermal growth factor homology modules of the human low-density lipoprotein receptor

The ligand-binding region of the low-density lipoprotein (LDL) receptor is formed by seven N-terminal, imperfect, cysteine-rich (LB) modules. This segment is followed by an epidermal growth factor precursor homology domain with two N-terminal, tandem, EGF-like modules that are thought to participate in LDL binding and recycling of the endocytosed receptor to the cell surface. EGF-A and the concatemer, EGF-AB, of these modules were expressed in Escherichia coli. Correct protein folding of EGF-A and the concatemer EGF-AB was achieved in the presence or absence of calcium ions, in contrast to the LB modules, which require them for correct folding. Homonuclear and heteronuclear H-1-N-15 NMR spectroscopy at 17.6 T was used to determine the three-dimensional structure of the concatemer. Both modules are formed by two pairs of short, anti-parallel beta -strands. In the concatemer, these modules have a fixed relative orientation, stabilized by calcium ion-binding and hydrophobic interactions at the interface. N-15 longitudinal and transverse relaxation rates, and {H-1}-N-15 heteronuclear NOEs were used to derive a model-free description of the backbone dynamics of the molecule. The concatemer appears relatively rigid, particularly near the calcium ion-binding site at the module interface, with an average generalized order parameter of 0.85 +/- 0.11. Some mutations causing familial hypercholesterolemia may now be rationalized. Mutations of D41, D43 and E44 in the EGF-B calcium ion-binding region may affect the stability of the linker and thus the orientation of the tandem modules. The diminutive core also provides little structural stabilization, necessitating the presence of disulfide bonds. The structure and dynamics of EGF-AB contrast with the N-terminal LB modules, which require calcium ions both for folding to form the correct disulfide connectivities and for maintenance of the folded structure, and are connected by highly mobile linking peptides. (C) 2001 Academic Press.

Solid-state NMR structure determination of melittin in a lipid environment

Solid-state C-13 NMR spectroscopy was used to investigate the three-dimensional structure of melittin as lyophilized powder and in ditetradecylphosphatidylcholine (DTPC) membranes. The distance between specifically labeled carbons in analogs [1-C-13]Gly3-[2-C-13]Ala4, [1-C-13]Gly3-[2-C-13]Leu6, [1-C-13]Leu13-[2-C-13]Ala15, [2-C-13]Leu13-[1-C-13]Ala15, and [1-C-13]Leu13-[2-C-13]Leu16 was measured by rotational resonance. As expected, the internuclear distances measured in [1-C-13]Gly3-[2-C-13]Ala4 and [1-C-13]Gly3-[2-C-13]Leu6 were consistent with alpha -helical structure in the N-terminus irrespective of environment. The Internuclear distances measured in [1-C-13]Leu13-[2-C-13]Ala15, [2-C-13]Leu13-[1-C-13]Ala15, and [1-C-13]Leu13-[2-C-13]Leu16 revealed, via molecular modeling, some dependence upon environment for conformation in the region of the bend in helical structure induced by Pro14. A slightly larger interhelical angle between the N- and C-terminal helices was indicated for peptide in dry or hydrated gel state DTPC (139 degrees -145 degrees) than in lyophilized powder (121 degrees -139 degrees) or crystals (129 degrees). The angle, however, is not as great as deduced for melittin in aligned bilayers of DTPC in the liquid-crystalline state (similar to 160 degrees) (R. Smith, F. Separovic, T. J. Milne, A. Whittaker, F. M. Bennett, B. A. Cornell, and A. Makriyannis, 1994, J. Mol, Biol 241:456-466). The study illustrates the utility of rotational resonance in determining local structure within peptide-lipid complexes.