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  • 1.
    Berndt, Kurt D
    University of Chicago, USA.
    Design, synthesis, and characterization of amphiphilic helical peptides as models of protein structure1989Doctoral thesis, monograph (Other academic)
  • 2. Caballero-Herrera, A
    et al.
    Nordstrand, Kerstin
    Södertörn University, School of Life Sciences.
    Berndt, Kurt D
    Södertörn University, School of Life Sciences. Karolinska Institutet.
    Nilsson, L
    Effect of urea on peptide conformation in water: Molecular dynamics and experimental characterization2005In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 89, no 2, p. 842-857Article in journal (Refereed)
    Abstract [en]

    Molecular dynamics simulations of a ribonuclease A C-peptide analog and a sequence variant were performed in water at 277 and 300 K and in 8 M urea to clarify the molecular denaturation mechanism induced by urea and the early events in protein unfolding. Spectroscopic characterization of the peptides showed that the C-peptide analog had a high alpha-helical content, which was not the case for the variant. In the simulations, interdependent side-chain interactions were responsible for the high stability of the alpha-helical C-peptide analog in the different solvents. The other peptide displayed alpha-helical unwinding that propagated cooperatively toward the N-terminal. The conformations sampled by the peptides depended on their sequence and on the solvent. The ability of water molecules to form hydrogen bonds to the peptide as well as the hydrogen bond lifetimes increased in the presence of urea, whereas water mobility was reduced near the peptide. Urea accumulated in excess around the peptide, to which it formed long-lived hydrogen bonds. The unfolding mechanisms induced by thermal denaturation and by urea are of a different nature, with urea-aqueous solutions providing a better peptide solvation than pure water. Our results suggest that the effect of urea on the chemical denaturation process involves both the direct and indirect mechanisms.

  • 3. Filling, C
    et al.
    Nordling, E
    Benach, J
    Berndt, Kurt D
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institute.
    Ladenstein, R
    Jörnvall, H
    Oppermann, U
    Structural role of conserved Asn179 in the short-chain dehydrogenase/reductase scaffold2001In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 289, no 3, p. 712-717Article in journal (Refereed)
    Abstract [en]

    Short-chain dehydrogenases/reductases (SDR) constitute a large family of enzymes found in all forms of life. Despite a low level of sequence identity, the three-dimensional structures determined display a nearly superimposable alpha/beta folding pattern. We identified a conserved asparagine residue located within strand betaF and analyzed its role in the short-chain dehydrogenase/reductase architecture. Mutagenetic replacement of Asn179 by Ala in bacterial 3 beta /17 beta -hydroxysteroid dehydrogenase yields a folded, but enzymatically inactive enzyme, which is significantly more resistant to denaturation by guanidinium hydrochloride. Crystallographic analysis of the wild-type enzyme at 1.2-Angstrom resolution reveals a hydrogen bonding network, including a buried and well-ordered water molecule connecting strands betaE to betaF, a common feature found in 16 of 21 known three-dimensional structures of the family. Based on these results, we hypothesize that in mammalian 11 beta -hydroxysteroid dehydrogenase the essential Asn-linked glycosylation site, which corresponds to the conserved segment, displays similar structural features and has a central role to maintain the SDR scaffold.

  • 4. Fischer, H
    et al.
    Zhang, X U
    O'Brien, K P
    Kylsten, Per
    Södertörn University, Avdelning Naturvetenskap.
    Engvall, E
    C7, a novel nucleolar protein, is the mouse homologue of the Drosophila late puff product L82 and an isoform of human OXR12001In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 281, no 3, p. 795-803Article in journal (Refereed)
    Abstract [en]

    The C7 gene was identified in a project aimed to characterize differential gene expression upon attachment of cells to extracellular matrix proteins in vitro. C7 is the homologue of Drosophila L82, a late puff gene (Stowers et al. (1999) Dev. Biol. 213, 116-130) and human OXR1, a gene, which protects cells against oxidation (Volkert et al. (2000) Proc. Natl. Acad. Sci. USA 97, 14530-14535). All are transcribed into multiple splice forms with a common 3' domain. Additional members of this novel gene family are found in a number of eukaryotic species. In the mouse, the C7 gene is highly and broadly expressed during development in at least 4 splice forms, 3 of which were sequenced. In the adult, the C7 gene is most highly expressed in brain and testis. Antibodies to recombinant C7 protein localized to nucleoli in a variety of cell types, suggesting that C7 may be involved in the formation or function of this important organelle.

  • 5. Funk, C
    et al.
    Wiklund, R
    Schröder, Wolfgang P
    Södertörn University, Avdelning Naturvetenskap.
    Jansson, C
    D1' centers are less efficient than normal photosystem II centers2001In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 505, no 1, p. 113-117Article in journal (Refereed)
    Abstract [en]

    One prominent difference between the photosystem II (PSII) reaction center protein D1 ' in Synechocystis 6803 and normal D1 is the replacement of Phe-186 in D1 with leucine in D1 '. Mutants of Synechocystis 6803 producing only D1 ', or containing engineered D1 proteins with Phe-186 substitutions, were analyzed by 77 K fluorescence emission spectra, chlorophyll a fluorescence induction yield and decay kinetics, and flash-induced oxygen evolution. Compared to D1-containing PSII centers, D1 ' centers exhibited a 50% reduction in variable chlorophyll a fluorescence yield, while the flash-induced O-2 evolution pattern was unaffected. In the F186 mutants, both the P680(+)/Q(A)(-) recombination and O-2 oscillation pattern were noticeably perturbed.

  • 6. Grimm, T
    et al.
    Teglund, Stephan
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    Tackels, D
    Sangiorgi, E
    Gurrieri, F
    Schwartz, C
    Toftgard, R
    Genomic organization and embryonic expression of Suppressor of Fused, a candidate gene for the split-hand/split-foot malformation type 32001In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 505, no 1, p. 13-17Article in journal (Refereed)
    Abstract [en]

    The genes for human and mouse Suppressor of Fused (SU(FU)/Su(Fu)) in the Hedgehog signaling pathway were characterized and found to contain 12 exons. Human SU(FU) localized on chromosome 10q24-25 between the markers D10S192 and AFM183XB12. We detected three additional SU(FU) isoforms, two of which have lost their ability to interact with the transcription factor GLI1. Expression analysis using whole mount in situ hybridization revealed strong expression of Su(Fu) in various mouse embryonic tissues. SU(FU) was considered a candidate gene for the split-hand/split-foot malformation type 3 (SHFM3). However, no alterations in the SU(FU) gene were found in SHFM3 patients.

  • 7. Kaumaya, P T P
    et al.
    Berndt, Kurt D
    University of Chicago, USA.
    Heidorn, D B
    Trewhella, J
    Kezdy, F J
    Goldberg, E
    Synthesis and Biophysical Characterization of Engineered Topographic Immunogenic Determinants with Alpha-Alpha-Topology1990In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 29, no 1, p. 13-23Article in journal (Refereed)
  • 8.
    Korayem, Ahmed M.
    et al.
    Stockholms universitet / Assiut University, Assiut, Egypt.
    Hauling, Thomas
    Stockholms universitet.
    Lesch, Christine
    Stockholms universitet.
    Fabbri, Marco
    University of Adelaide, Glen Osmond, Australia.
    Lindgren, Malin
    Södertörn University, School of Life Sciences. Stockholms universitet.
    Loseva, Olga
    Stockholms universitet.
    Schmidt, Otto
    University of Adelaide, Glen Osmond, Australia.
    Dushay, Mitchell S.
    Södertörn University, School of Life Sciences. Uppsala University.
    Theopold, Ulrich
    Stockholms universitet.
    Evidence for an immune function of lepidopteran silk proteins2007In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 352, no 2, p. 317-322Article in journal (Refereed)
    Abstract [en]

    Hemolymph coagulation stops bleeding and protects against infection. Clotting factors include both proteins that are conserved during evolution as well as more divergent proteins in different species. Here we show that several silk proteins also appear in the clot of the greater wax moth Galleria mellonella. RT-PCR analysis reveals that silk proteins are expressed in immune tissues and induced upon wounding in both Galleria and Ephestia kuehniella, a second pyralid moth. Our results support the idea that silk proteins were co-opted for immunity and coagulation during evolution.

  • 9.
    Larsson, Sofia L
    et al.
    Södertörn University, Avdelning Naturvetenskap. Stockholm University.
    Sloma, Marika S
    Södertörn University, Avdelning Naturvetenskap. Stockholm University.
    Nygård, Odd
    Södertörn University, Avdelning Naturvetenskap.
    Conformational changes in the structure of domains II and V of 28S rRNA in ribosomes treated with the translational inhibitors ricin or alpha-sarcin2002In: Biochimica et Biophysica Acta, Gene Structure and Expression, ISSN 0167-4781, E-ISSN 1879-2634, Vol. 1577, no 1, p. 53-62Article in journal (Refereed)
    Abstract [en]

    Ricin and alpha-sarcin modify neighbouring sites in the so-called sarcin/ricin (S/R) loop of 28S rRNA, thereby destroying the necessary dynamic flexibility of the ribosome, and inhibiting the elongation factor assisted steps of the elongation cycle. The effects of the two translational inhibitors on the conformation of domains 11 and V of 28 S rRNA were investigated by chemical modification of programmed mouse ribosomes pretreated with ricin or alpha-sarcin. The results showed that the two ribosome-inactivating proteins (RIP) influenced the structure of the ribosomal RNA. Inhibitor-affected sites were located at or near sites previously proposed to be involved in functional domains. The modification patterns obtained after ricin or alpha-sarcin treatment of ribosomes were partially overlapping. However, there were several inhibitor-specific structural changes in 28S rRNA. Such changes were found at positions located at the GTPase activating centre of the ribosome and in the S/R domain, indicating that the structure in these regions of the ribosomes differed after treatment with the two inhibitors. These changes are consistent with ricin and alpha-sarcin having specific effects on eEF-2 and eEF-1 interaction with the ribosome, respectively.

  • 10.
    Miranda-Vizuete, Antonio
    et al.
    Södertörn University, School of Life Sciences.
    Fierro Gonzalez, Juan Carlos
    Södertörn University, School of Life Sciences.
    Gahmon, Gabriele
    Burghoorn, Jan
    Södertörn University, School of Life Sciences.
    Navas, Plácido
    Swoboda, Peter
    Södertörn University, School of Life Sciences.
    Lifespan decrease in a Caenorhabditis elegans mutant lacking TRX-1, a thioredoxin expressed in ASJ sensory neurons2006In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 580, no 2, p. 484-490Article in journal (Refereed)
    Abstract [en]

    Thioredoxins are a class of small proteins that play a key role in regulating many cellular redox processes. We report here the characterization of the first member of the thioredoxin family in metazoans that is mainly associated with neurons. The Caenorhabditis elegans gene B0228.5 encodes a thioredoxin (TRX-1) that is expressed in ASJ ciliated sensory neurons, and to some extent also in the posterior-most intestinal cells. TRX-1 is active at reducing protein disulfides in the presence of a heterologous thioredoxin reductase. A mutant worm strain carrying a null allele of the trx-1 gene displays a reproducible decrease in both mean and maximum lifespan when compared to wild-type. The identification and characterization of TRX-1 paves the way to use C elegans as an in vivo model to study the role of thioredoxins in lifespan and nervous system physiology and pathology.

  • 11.
    Petersson, Ulrika A.
    et al.
    Södertörn University, School of Life Sciences.
    Kieselbach, Thomas
    Garcia-Cerdan, Jose G.
    Schroder, Wolfgang P.
    The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome2006In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 580, no 26, p. 6055-6061Article in journal (Refereed)
    Abstract [en]

    Peroxiredoxins; have been discovered in many organisms ranging from eubacteria to mammals, and their known biological functions include both oxidant defense and signal transduction. The genome of Arabidopsis thaliana encodes for ten individual peroxiredoxins, of which four are located in the chloroplast. The best-characterized member of the chloroplast peroxiredoxins is 2-Cys Prx that is associated with the stroma side of the thylakoid membrane and is considered to participate in antioxidant defense and protection of photosynthesis. This study addressed the chloroplast peroxiredoxin Prx Q and showed that its subcellular location is the lumen of the thylakoid membrane. To get insight in the biological function of the Prx Q protein of Arabidopsis, the protein levels of the Prx Q protein in thylakoid membranes were studied under different light conditions and oxidative stress. A T-DNA knockout mutant of Prx Q did not show any visible phenotype and had normal photosynthetic performance with a slightly increased oxygen evolving activity.

  • 12.
    Sagemark, Johan
    et al.
    Södertörn University, School of Life Sciences. Karolinska Institute.
    Elgan, Tobias H.
    Södertörn University, School of Life Sciences. Karolinska Institute.
    Bürglin, Thomas R.
    Södertörn University, School of Life Sciences. Karolinska Institute.
    Johansson, Catrine
    Holmgren, Arne
    Berndt, Kurt D.
    Södertörn University, School of Life Sciences. Karolinska Institute.
    Redox properties and evolution of human glutaredoxins2007In: Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, E-ISSN 1097-0134, Vol. 68, no 4, p. 879-892Article in journal (Refereed)
    Abstract [en]

    Glutaredoxins (Grxs) are glutathione-dependent oxidoreductases that belong to the thioredoxin superfamily catalyzing thiol-disulfide exchange reactions via active site cysteine residues. Focusing on the human dithiol glutaredoxins having a C-X-Y-C active site sequence motif, the redox potentials of hGrxl and hGrx2 were determined to be -232 and -221 mV, respectively, using a combination of redox buffers, protein-protein equilibrium and thermodynamic linkage. In addition, a nonactive site disulfide was identified between Cys28 and Cys.113 in hGrx2 using redox buffers and chemical digestion. This disulfide confers nearly five kcal mol-1 additional stability by linking the C-terminal helix to the bulk of the protein. The redox potential of this nonactive site disulfide was determined to be -317 mVand is thus expected to be present in all but the most reducing conditions in vivo. As all human glutaredoxins contain additional nonactive site cysteine residues, a full phylogenetic analysis was performed to help elucidate their structural and functional roles. Three distinct groups were found: Grx1, Grx2, and Grx5, the latter representing a highly conserved group of monothiol glutaredoxins having a C-G-F-S active site sequence, with clear homologs from bacteria to human. Grx1 and Grx2 diverged from a common ancestor before the origin vertebrates, possibly even earlier in animal evolution. The highly stabilizing nonactive site disulfide observed in hGrx2 is found to be a conserved feature within the deuterostomes and appears to be the only additional conserved intramolecular disulfide within the glutaredoxins.

  • 13. Tjernberg, L O
    et al.
    Pramanik, A
    Björling, S
    Thyberg, P
    Thyberg, J
    Nordstedt, C
    Berndt, Kurt D
    Karolinska Institutet.
    Terenius, L
    Rigler, R
    Amyloid beta-peptide polymerization studied using fluorescence correlation spectroscopy1999In: Chemistry and Biology, ISSN 1074-5521, E-ISSN 1879-1301, Vol. 6, no 1, p. 53-62Article in journal (Refereed)
    Abstract [en]

    Background: The accumulation of fibrillar deposits of amyloid beta-peptide (A beta) in brain parenchyma and cerebromeningeal blood vessels is a key step in the pathogenesis of Alzheimer's disease. In this report, polymerization of A beta was studied using fluorescence correlation spectroscopy (FCS), a technique capable of detecting small molecules and large aggregates simultaneously in solution. Results: The polymerization of A beta dissolved in Tris-buffered saline, pH 7.4, occurred above a critical concentration of 50 mu M and proceeded from monomers/dimers into two discrete populations of large aggregates, without any detectable amount of oligomers. The aggregation showed very high cooperativity and reached a maximum after 40 min, followed by an increase in the amount of monomers/dimers and a decrease in the size of the large aggregates. Electron micrographs of samples prepared at the time for maximum aggregation showed a mixture of an amorphous network and short diffuse fibrils, whereas only mature amyloid fibrils were detected after one day of incubation. The aggregation was reduced when A beta was incubated in the presence of A beta ligands, oligopeptides previously shown to inhibit fibril formation, and aggregates were partly dissociated after the addition of the ligands. Conclusions: The polymerization of A beta is a highly cooperative process in which the formation of very large aggregates precedes the formation of fibrils. The entire process can be inhibited and, at least in early stages, partly reversed by A beta ligands.

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