2 resultados para solid-state nuclear magnetic resonance
em eResearch Archive - Queensland Department of Agriculture
Resumo:
Increasing organic carbon inputs to agricultural soils through the use of pastures or crop residues has been suggested as a means of restoring soil organic carbon lost via anthropogenic activities, such as land use change. However, the decomposition and retention of different plant residues in soil, and how these processes are affected by soil properties and nitrogen fertiliser application, is not fully understood. We evaluated the rate and extent of decomposition of 13C-pulse labelled plant material in response to nitrogen addition in four pasture soils of varying physico-chemical characteristics. Microbial respiration of buffel grass (Cenchrus ciliaris L.), wheat (Triticum aestivum L.) and lucerne (Medicago sativa L.) residues was monitored over 365-days. A double exponential model fitted to the data suggested that microbial respiration occurred as an early rapid and a late slow stage. A weighted three-compartment mixing model estimated the decomposition of both soluble and insoluble plant 13C (mg C kg−1 soil). Total plant material decomposition followed the alkyl C: O-alkyl C ratio of plant material, as determined by solid-state 13C nuclear magnetic resonance spectroscopy. Urea-N addition increased the decomposition of insoluble plant 13C in some soils (≤0.1% total nitrogen) but not others (0.3% total nitrogen). Principal components regression analysis indicated that 26% of the variability of plant material decomposition was explained by soil physico-chemical characteristics (P = 0.001), which was primarily described by the C:N ratio. We conclude that plant species with increasing alkyl C: O-alkyl C ratio are better retained as soil organic matter, and that the C:N stoichiometry of soils determines whether N addition leads to increases in soil organic carbon stocks.
Resumo:
The caseins (αs1, αs2, β, and κ) are phosphoproteins present in bovine milk that have been studied for over a century and whose structures remain obscure. Here we describe the chemical synthesis and structure elucidation of the N-terminal segment (1–44) of bovine κ-casein, the protein which maintains the micellar structure of the caseins. κ-Casein (1–44) was synthesised by highly optimised Boc solid-phase peptide chemistry and characterised by mass spectrometry. Structure elucidation was carried out by circular dichroism and nuclear magnetic resonance spectroscopy. CD analysis demonstrated that the segment was ill defined in aqueous medium but in 30% trifluoroethanol it exhibited considerable helical structure. Further, NMR analysis showed the presence of a helical segment containing 26 residues which extends from Pro8 to Arg34. This is the first report which demonstrates extensive secondary structure within the casein class of proteins.