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Kurt Nielsen

Publications and source records attributed to Kurt Nielsen.

10 recordsLinked to original sources

Reducing nitrogen loading of inland and marine waters--evaluation of Danish policy measures to reduce nitrogen loss from farmland.

An evaluation in December 2003 of the Danish National Action Plan for the Aquatic Environment II showed that nitrogen leaching from farmland had declined to almost half the amount of that in 1989. This can be ascribed to successful implementation of several measures, the most efficient of which were related to the use of fertilizers: lowered nitrogen standards for crops, increased nitrogen utilization in manure and catch crops. Although the objectives of the plan were almost met and measurements have shown a similar, but not percentually as high a decrease in nitrogen concentrations in both inland and coastal waters, the ecological impact in estuaries and coastal areas is not yet satisfactorily significant. As a consequence, a new National Action Plan for the Aquatic Environment III, including both nitrogen and phosphorus reduction from farming, was agreed to in April 2004. To ensure that good ecological status can be achieved in water bodies according to the requirements of the European Union Water Framework Directive, the national measures will be combined with additional measures for individual river basins.

Agriculture↗

Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: implications for function and misfunction.

The aqueous solution structure of the full-length recombinant ovine prion protein PrP(25-233), together with that of the N-terminal truncated version PrP(94-233), have been studied using vibrational Raman optical activity (ROA) and ultraviolet circular dichroism (UVCD). A sharp positive band at approximately 1315 cm(-1) characteristic of poly(L-proline) II (PPII) helix that is present in the ROA spectrum of the full-length protein is absent from that of the truncated protein, together with bands characteristic of beta-turns. Although it is not possible similarly to identify PPII helix in the full-length protein directly from its UVCD spectrum, subtraction of the UVCD spectrum of PrP(94-233) from that of PrP(25-233) yields a difference UVCD spectrum also characteristic of PPII structure and very similar to the UVCD spectrum of murine PrP(25-113). These results provide confirmation that a major conformational element in the N-terminal region is PPII helix, but in addition show that the PPII structure is interspersed with beta-turns and that little PPII structure is present in PrP(94-233). A principal component analysis of the ROA data indicates that the alpha-helix and beta-sheet content, located in the structured C-terminal domain, of the full-length and truncated proteins are similar. The flexibility imparted by the high PPII content of the N-terminal domain region may be an essential factor in the function and possibly also the misfunction of prion proteins.

Amino Acid Sequence↗

Crystal structure and spectroscopic characterization of K8(VO)2O(SO4)6.

Red and yellow dichroistic crystals of a vanadium(V) compound, potassium (mu-oxo, di-mu-sulfato)bis(oxodisulfatovanadate), K(8)(VO)(2)O(SO(4))(6), have been obtained from the ternary catalytic model melt system K(2)S(2)O(7)[bond]K(2)SO(4)[bond]V(2)O(5). By slow cooling of the melt from 420 to 355 degrees C, crystal growth occurred, using solid V(2)O(5) crystals present in the melt as nucleation promoter. The compound crystallizes in the monoclinic space group P2(l) with a = 13.60(9) A, b = 13.93(9) A, c = 14.05(9) A, beta = 90.286(10) degrees, and Z = 2. It contains two VO(6) octahedra linked together by a mu-oxo and two mu-sulfato bridges. Furthermore, each octahedron has two monodentate sulfate ligands, making the dimeric entity coordinatively saturated. IR spectroscopy shows bands arising from V[bond]O[bond]V and V[double bond]O stretches as well as splitting of sulfate bands due to the different degrees of freedom present for different conformations of sulfate ligands. The coordination of vanadium in K(8)(VO)(2)O(SO(4))(6) is discussed in relation to the reaction mechanism of SO(2) oxidation catalysis.

Journal Article↗

A new perspective on beta-sheet structures using vibrational Raman optical activity: from poly(L-lysine) to the prion protein.

The vibrational Raman optical activity (ROA) spectrum of a polypeptide in a model beta-sheet conformation, that of poly(l-lysine), was measured for the first time, and the alpha-helix --> beta-sheet transition monitored as a function of temperature in H(2)O and D(2)O. Although no significant population of a disordered backbone state was detected at intermediate temperatures, some side chain bands not present in either the alpha-helix or beta-sheet state were observed. The observation of ROA bands in the extended amide III region assigned to beta-turns suggests that, under our experimental conditions, beta-sheet poly(L-lysine) contains up-and-down antiparallel beta-sheets based on the hairpin motif. The ROA spectrum of beta-sheet poly(L-lysine) was compared with ROA data on a number of native proteins containing different types of beta-sheet. Amide I and amide II ROA band patterns observed in beta-sheet poly(L-lysine) are different from those observed in typical beta-sheet proteins and may be characteristic of an extended flat multistranded beta-sheet, which is unlike the more irregular and twisted beta-sheet found in most proteins. However, a reduced isoform of the truncated ovine prion protein PrP(94-233) that is rich in beta-sheet shows amide I and amide II ROA bands similar to those of beta-sheet poly(L-lysine), which suggests that the C-terminal domain of the prion protein is able to support unusually flat beta-sheets. A principal component analysis (PCA) that identifies protein structural types from ROA band patterns provides a useful representation of the structural relationships among the polypeptide and protein states considered in the study.

Animals↗

New insight into the solution structures of wheat gluten proteins from Raman optical activity.

Vibrational Raman optical activity (ROA) spectra of the wheat proteins alpha-gliadin (A-gliadin), omega-gliadin, and a 30 kDa peptide called T-A-1 from the high molecular weight glutenin subunit (HMW-GS) Dx5 were measured to obtain new information about their solution structures. The spectral data show that, under the conditions investigated, A-gliadin contains a considerable amount of hydrated alpha-helix, most of which probably lies within a relatively structured C-terminal domain. Smaller quantities of beta-structure and poly(l-proline) II (PPII) helix were also identified. Addition of methanol was found to increase the alpha-helix content at the expense of some of the beta and PPII structure. In comparison, omega-gliadin and the T-A-1 peptide were found to consist of large amounts of well-defined PPII structure with some turns but no alpha-helix. The results for the T-A-1 peptide are in agreement with a model in which HMW-GS are extended but not highly rigid. Application of a pattern recognition technique, based on principal component analysis (PCA), to the ROA spectra reinforces these conclusions.

Amino Acid Sequence↗

Assessing reference conditions according to the European Water Framework Directive using modelling and analysis of historical data: an example from Randers Fjord, Denmark.

The European Water Framework Directive (WFD) requires the definition of reference conditions, i.e. pristine conditions, for all surface waters. As the present state of Danish coastal waters cannot be referred to as pristine, reference conditions have to be assessed by analysis of historical data or by the use of models. Using Randers Fjord as an example, the aim of this work was i) to demonstrate possibilities and restrictions of assessing reference conditions by historical data and by modelling; and ii) to demonstrate how ecological conditions have changed along with eutrophication. The ample historical data from Randers Fjord allowed us to assess reference conditions with respect to benthic macrophytes and benthic fauna. Models of varying complexity enabled us to assess reference conditions for nutrients, chlorophyll a, Secchi depth, and eelgrass. We conclude that models can be a useful supplement to assess reference conditions, though they are presently restricted by the lack of quantitative links between eutrophication and species composition.

Animals↗

Solution structures of potato virus X and narcissus mosaic virus from Raman optical activity.

Potato virus X (PVX) and narcissus mosaic virus (NMV) were studied using vibrational Raman optical activity (ROA) in order to obtain new information on the structures of their coat protein subunits. The ROA spectra of the two intact virions are very similar to each other and similar to that of tobacco mosaic virus (TMV) studied previously, being dominated by signals characteristic of proteins with helix bundle folds. In particular, PVX and NMV show strong positive ROA bands at approximately 1340 cm(-1) assigned to hydrated alpha-helix and perhaps originating in surface exposed helical residues, together with less strong positive ROA intensity in the range approximately 1297-1312 cm(-1) assigned to alpha-helix in a more hydrophobic environment and perhaps originating in residues at helix-helix interfaces. The positive approximately 1340 cm(-1) ROA band of TMV is less intense than those of PVX and NMV, suggesting that TMV contains less hydrated alpha-helix. Small differences in other spectral regions reflect differences in some loop, turn and side-chain compositions and conformations among the three viruses. A pattern recognition program based on principal component analysis of ROA spectra indicates that the coat protein subunit folds of PVX and NMV may be very similar to each other and similar to that of TMV. These results suggest that PVX and NMV may have coat protein subunit structures based on folds similar to the TMV helix bundle and hence that the helical architecture of the PVX and NMV particles may be similar to that of TMV but with different structural parameters.

Capsid↗

Molecular structures of viruses from Raman optical activity.

A vibrational Raman optical activity (ROA) study of a range of different structural types of virus exemplified by filamentous bacteriophage fd, tobacco mosaic virus, satellite tobacco mosaic virus, bacteriophage MS2 and cowpea mosaic virus has revealed that, on account of its sensitivity to chirality, ROA is an incisive probe of their aqueous solution structures at the molecular level. Protein ROA bands are especially prominent from which, as we have shown by comparison with the ROA spectra of proteins with known structures and by using a pattern recognition program, the folds of the major coat protein subunits may be deduced. Information about amino acid side-chain conformations, exemplified here by the determination of the sign and magnitude of the torsion angle chi(2,1) for tryptophan in fd, may also sometimes be obtained. By subtracting the ROA spectrum of the empty protein capsid (top component) of cowpea mosaic virus from those of the intact middle and bottom-upper components separated by means of a caesium chloride density gradient, the ROA spectrum of the viral RNA was obtained, which revealed that the RNA takes up an A-type single-stranded helical conformation and that the RNA conformations in the middle and bottom-upper components are very similar. This information is not available from the X-ray crystal structure of cowpea mosaic virus since no nucleic acid is visible.

Bacteriophage M13↗

Crystal Structure and Spectroscopic Characterization of K(6)(VO)(4)(SO(4))(8) Containing Mixed-Valent Vanadium(IV)-Vanadium(V).

Pleochroistic crystals (dark green to colorless) of a mixed-valence V(IV)-V(V) compound, K(6)(VO)(4)(SO(4))(8), suitable for X-ray determination have been obtained from the catalytically important K(2)S(2)O(7)-V(2)O(5)/SO(2)-O(2)-SO(3)-N(2) molten salt-gas system, at approximately 400 degrees C. The compound crystallizes in the monoclinic space group P2(1) (No. 4) with a = 8.931(2) Å, b = 18.303 (3) Å, c = 9.971(2) Å, beta = 90.11(2) degrees, and Z = 2. It contains two rather similar V(IV)-V(V) pairs of VO(6) octahedra distorted as usual having a short V-O bond of around 1.57 Å, a long bond of around 2.40 Å trans to this, and four equatorial bonds around 2.00 Å. The bond lengths of the V(V)O(6) octahedra are significantly shorter than those found for the V(IV)O(6) octahedra. The eight different SO(4)(2)(-) groups are all bridging bidentate between the V(IV) and V(V) atoms; a third oxygen is coordinated to a vanadium atom of a neighboring chain trans to the short V=O bond, and the fourth oxygen remains uncoordinated. The measured bond distances and angles show a considerable distortion of the SO(4) tetrahedra. This is confirmed by the IR spectra of the compound, where large shift and splitting of the sulfate nu(3) bands up to wave numbers of around 1300 cm(-)(1) is observed. The ESR spectra of the compound exhibit weak anisotropy with g(iso) = 1.972 +/- 0.002 and DeltaB(pp) = 65 +/- 2 G. The compound may cause the deactivation for industrial sulfuric acid catalysts observed around 400 degrees C in highly converted SO(2)-O(2)-N(2) gas mixtures.

Journal Article↗

Experimental pain stimulates respiration and attenuates morphine-induced respiratory depression: a controlled study in human volunteers.

Although evidence is lacking, clinical experience suggests that pain stimulation acts as a respiratory stimulant and antagonises opioid-induced respiratory depression. The present study examined the effects of experimental pain stimulation on the ventilatory response to CO2 and morphine-induced respiratory depression. Pain was induced by a modification of the Tourniquet Pain Technique and changes in ventilatory parameters were registered through monitoring of the CO2 response of tidal volume, minute ventilation, respiratory rate and mouth occlusion pressure. The ventilatory parameters were obtained before and during pain stimulation and repeated after the administration of morphine and finally after naloxone. In the present investigation experimental pain-stimulated respiration and attenuated morphine-induced respiratory depression. Only changes in the intercept values of the CO2 response were observed. The slopes of the CO2-response curves were not affected. These observations suggested that both pain stimulation and morphine administration altered the threshold of the respiratory centre to CO2 stimulation. Naloxone administration was the only intervention altering the sensitivity of the respiratory centre to CO2. These results suggest that pain stimulates respiration and attenuates morphine-induced respiratory depression.

Adult↗