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  • 1.
    Ahlgren, Joakim
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry, Analytical Chemistry.
    Tranvik, Lars
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Ecology and Evolution, Limnology.
    Gogoll, Adolf
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry, Organic Chemistry I.
    Waldebäck, Monica
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry, Analytical Chemistry.
    Markides, Karin
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry, Analytical Chemistry.
    Rydin, Emil
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Ecology and Evolution, Limnology.
    Sediment Depth Attenuation of Biogenic Phosphorus Compounds Measured by 31P NMR2005In: Environmental Science and Technology, ISSN 0013-936X, E-ISSN 1520-5851, Vol. 39, no 3, p. 867-872Article in journal (Refereed)
    Abstract [en]

    Being a major cause of eutrophication and subsequent loss of water quality, the turnover of phosphorus (P) in lake sediments is in need of deeper understanding. A major part of the flux of P to eutrophic lake sediments is organically bound or of biogenic origin. This P is incorporated in a poorly described mixture of autochthonous and allochthonous sediment and forms the primary storage of P available for recycling to the water column, thus regulating lake trophic status. To identify and quantify biogenic sediment P and assess its lability, we analyzed sediment cores from Lake Erken, Sweden, using traditional P fractionation, and in parallel, NaOH extracts were analyzed using 31P NMR. The surface sediments contain orthophosphates (ortho-P) and pyrophosphates (pyro-P), as well as phosphate mono- and diesters. The first group of compounds to disappear with increased sediment depth is pyrophosphate, followed by a steady decline of the different ester compounds. Estimated half-life times of these compound groups are about 10 yr for pyrophosphate and 2 decades for mono- and diesters. Probably, these compounds will be mineralized to ortho-P and is thus potentially available for recycling to the water column, supporting further growth of phytoplankton. In conclusion, 31P NMR is a useful tool to asses the bioavailability of certain P compound groups, and the combination with traditional fractionation techniques makes quantification possible.

  • 2. Aili, Daniel
    et al.
    Enander, Karin
    Baltzer, Lars
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry.
    Liedberg, Bo
    Synthetic de novo designed polypeptides for control of nanoparticle assembly and biosensing2007In: Biochemical Society Transactions, ISSN 0300-5127, E-ISSN 1470-8752, Vol. 35, no 3, p. 532-534Article in journal (Refereed)
    Abstract [en]

    This contribution describes how de novo designed synthetic helix–loop–helix polypeptides are utilized tocontrol the assembly of gold nanoparticles and as scaffolds for biosensing. The synthetic polypeptides aredesigned to fold into a four-helix bundle upon dimerization. When immobilized on gold nanoparticles,dimerization and folding occur between peptides on neighbouring particles as an effect of particleaggregation and the folded polypeptides are rigid enough to keep the particles separated at a distancecorresponding to the size of the four-helix bundle. Moreover, peptide dimerization offers a convenientroute to assemble nanoparticles into hybrid multilayers on planar substrates. The drastic change in theresonance conditions of the localized nanoparticle surface plasmon upon particle aggregation is shown tobe useful for optical detection of biomolecular interactions.

  • 3. Hederos, Sofia
    et al.
    Broo, Kerstin S
    Jakobsson, Emma
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Chemistry, Department of Biochemistry and Organic Chemistry, Biochemistry. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology. ICM.
    Kleywegt, Gerard J
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Chemistry, Department of Biochemistry and Organic Chemistry, Biochemistry. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology. ICM.
    Mannervik, Bengt
    Department of Biochemistry. Chemistry, Department of Biochemistry and Organic Chemistry, Biochemistry. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
    Baltzer, Lars
    Department of Chemistry. Chemistry, Department of Biochemistry and Organic Chemistry, Biochemistry. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
    Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1.2004In: Proc Natl Acad Sci U S A, ISSN 0027-8424, Vol. 101, no 36, p. 13163-7Article in journal (Refereed)
    Abstract [en]

    A strategy for rational enzyme design is reported and illustrated by the engineering of a protein catalyst for thiol-ester hydrolysis. Five mutants of human glutathione (GSH; gamma-Glu-Cys-Gly) transferase A1-1 were designed in the search for a catalyst and to provide a set of proteins from which the reaction mechanism could be elucidated. The single mutant A216H catalyzed the hydrolysis of the S-benzoyl ester of GSH under turnover conditions with a k(cat)/K(M) of 156 M(-1) x min(-1), and a catalytic proficiency of >10(7) M(-1) when compared with the first-order rate constant of the uncatalyzed reaction. The wild-type enzyme did not hydrolyze the substrate, and thus, the introduction of a single histidine residue transformed the wild-type enzyme into a turnover system for thiol-ester hydrolysis. By kinetic analysis of single, double, and triple mutants, as well as from studies of reaction products, it was established that the enzyme A216H catalyzes the hydrolysis of the thiol-ester substrate by a mechanism that includes an acyl intermediate at the side chain of Y9. Kinetic measurements and the crystal structure of the A216H GSH complex provided compelling evidence that H216 acts as a general-base catalyst. The introduction of a single His residue into human GSH transferase A1-1 created an unprecedented enzymatic function, suggesting a strategy that may be of broad applicability in the design of new enzymes. The protein catalyst has the hallmarks of a native enzyme and is expected to catalyze various hydrolytic, as well as transesterification, reactions.

  • 4.
    Sunnerheim, Kerstin
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry.
    Nordqvist, Anneli
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry.
    Nordlander, Göran
    Borg-Karlson, Anna-Karin
    Unelius, Rickard
    Bohman, Björn
    Nordenhem, Henrik
    Hellqvist, Claes
    Karlén, Anders
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry.
    Quantitative structure-activity relationships of pine weevil antifeedants, a multivariate approach2007In: Journal of Agricultural and Food Chemistry, ISSN 0021-8561, E-ISSN 1520-5118, Vol. 55, no 23, p. 9365-9372Article in journal (Refereed)
    Abstract [en]

    Antifeedant activity of mainly phenylpropanoic, cinnamic, and benzoic acids esters was tested on the pine weevil, Hylobius abietis (L.). Of 105 compounds screened for activity, 9 phenylpropanoates, 3 cinnamates, and 4 benzoates were found to be highly active antifeedants. To understand the structure–activity relationships of these compounds, a multivariate analysis study was performed. A number of molecular and substituent descriptors were calculated and correlated to results from two-choice feeding tests with H. abietis. Three local models were developed that had good internal predictive ability. External test sets showed moderate predictivity. In general, low polarity, small size, and high lipophilicity were characteristics for compounds having good antifeedant activity.

1 - 4 of 4
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