Search Results - "DAMASCHUN, H"

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  1. 1

    Effect of environmental conditions on aggregation and fibril formation of barstar by Gast, K, Modler, A J, Damaschun, H, Kröber, R, Lutsch, G, Zirwer, D, Golbik, R, Damaschun, G

    Published in European biophysics journal (01-12-2003)
    “…The dependence on environmental conditions of the assembly of barstar into amyloid fibrils was investigated starting from the nonnative, partially folded state…”
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  2. 2

    Denatured states of yeast phosphoglycerate kinase by Damaschun, G, Damaschun, H, Gast, K, Zirwer, D

    Published in Biochemistry (Moscow) (01-03-1998)
    “…Structures of proteins in unfolded states have important implications for the protein folding problem and for the translocation of polypeptide chains…”
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    Effect of platinum(II) chemotherapeutic agents on properties of DNA liquid crystals by Yevdokimov YuM, Skuridin, S G, Salyanov, V I, Damaschun, G, Damaschun, H, Misselwitz, R, Kleinwächter, V

    Published in Biophysical chemistry (01-04-1990)
    “…We have investigated the X-ray and optical properties (CD spectra and polarization microscopy) of liquid-crystalline phases and dispersions formed on…”
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  5. 5

    Proteins can adopt totally different folded conformations by Damaschun, G, Damaschun, H, Gast, K, Zirwer, D

    Published in Journal of molecular biology (20-08-1999)
    “…The three-dimensional structure of a protein is determined by interactions between its amino acids and by interactions of the amino acids with molecules of the…”
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  6. 6

    Prothymosin .alpha.: A Biologically Active Protein with Random Coil Conformation by Gast, Klaus, Damaschun, Hilde, Eckert, Klaus, Schulze-Forster, Kai, Maurer, H. Rainer, Mueller-Frohne, Marlies, Zirwer, Dietrich, Czarnecki, Jan, Damaschun, Gregor

    Published in Biochemistry (Easton) (10-10-1995)
    “…Prothymosin is an acidic protein with an unusual amino acid composition. Though its exact function is not yet known, its high evolutionary conservation and…”
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  7. 7

    Conversion of yeast phosphoglycerate kinase into amyloid-like structure by Damaschun, Gregor, Damaschun, Hilde, Fabian, Heinz, Gast, Klaus, Kröber, Reinhard, Wieske, Martin, Zirwer, Dietrich

    “…Yeast phosphoglycerate kinase is a structurally well‐characterized enzyme consisting of 415 amino acids without disulfide bonds. Anion‐induced refolding from…”
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  8. 8

    X-ray small-angle scattering study of mononucleosomes and of the close packing of nucleosomes in polynucleosomes by Damaschun, H, Damaschun, G, Pospelov, V A, Vorob'ev, V I

    Published in Molecular biology reports (31-10-1980)
    “…The radius of gyration of mononucleosomes determined by X-ray small-angle scattering is 4.35 nm. The maximum dimension determined from the distance…”
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    Compactness of protein molten globules: temperature-induced structural changes of the apomyoglobin folding intermediate by Gast, K, Damaschun, H, Misselwitz, R, Müller-Frohne, M, Zirwer, D, Damaschun, G

    Published in European biophysics journal (01-10-1994)
    “…Apomyoglobin undergoes a two-step unfolding transition when the pH is lowered from 6 to 2. The partly folded intermediate (I) state at pH 4 and low ionic…”
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  11. 11

    X-ray scattering evidence that calf thymus DNA in solution is a double helix and not a warped zipper by Müller, J J, Damaschun, G, Damaschun, H, Misselwitz, R, Zirwer, D, Nothnagel, A

    Published in Biomedica biochimica acta (1984)
    “…Isotropic X-ray scattering experiments with calf thymus DNA in solution under B-form conditions were used to differentiate between the double helical and the…”
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  12. 12

    Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast by Damaschun, Gregor, Damaschun, Hilde, Gast, Klaus, Misselwitz, Rolf, Mueller, Juergen J, Pfeil, Wolfgang, Zirwer, Dietrich

    Published in Biochemistry (Easton) (03-08-1993)
    “…The temperature-dependent conformational equilibrium of 3-phosphoglycerate kinase has been studied in the temperature range from 1 to 30 degrees C by means of…”
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  13. 13

    How many base-pairs per turn does DNA have in solution and in chromatin? An answer from wide-angle X-ray scattering by Damaschun, G, Damaschun, H, Misselwitz, R, Pospelov, V A, Zalenskaya, I A, Zirwer, D, Müller, J J, Vorobev, V I

    Published in Biomedica biochimica acta (1983)
    “…Experimental excess wide-angle X-ray scattering curves from DNA in solution, from Na-DNA crystallites in mother-liquor, from mononucleosomes in solution and…”
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  14. 14

    Cold denaturation of yeast phosphoglycerate kinase: Kinetics of changes in secondary structure and compactness on unfolding and refolding by Gast, Klaus, Damaschun, Gregor, Damaschun, Hilde, Misselwitz, Rolf, Zirwer, Dietrich

    Published in Biochemistry (Easton) (03-08-1993)
    “…Under mildly destabilizing conditions (0.7 M GuHCl), phosphoglycerate kinase from yeast undergoes a reversible two-step equilibrium unfolding transition when…”
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  15. 15

    Ribonuclease T1 has different dimensions in the thermally and chemically denatured states: a dynamic light scattering study by Gast, Klaus, Zirwer, Dietrich, Damaschun, Hilde, Hahn, Ulrich, Müller-Frohne, Marlies, Wirth, Matthias, Damaschun, Gregor

    Published in FEBS letters (24-02-1997)
    “…Ribonuclease T1 can be unfolded and refolded without forming noticeable amounts of aggregates allowing to characterise the dimensions of a protein in different…”
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  16. 16

    Streptokinase is a flexible multi-domain protein by DAMASCHUN, G, DAMASCHUN, H, GAST, K, GERLACH, D, MISSELWITZ, R, WELFLE, H, ZIRWER, D

    Published in European biophysics journal (1992)
    “…The structure of streptokinase in solution has been studied by dynamic light scattering, small-angle X-ray scattering and circular dichroism spectroscopy. The…”
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  17. 17

    Solvent dependence of dimensions of unfolded protein chains by Damaschun, G, Damaschun, H, Gast, K, Zirwer, D, Bychkova, V E

    “…The radii of gyration of unfolded apo-cytochrome C at pH 2.3 have been determined in three conditions: (i) 20 mM sodium phosphate buffer; (ii) 0.25 M NaCl; and…”
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  18. 18

    Conformation of thermally denatured RNase T1 with intact disulfide bonds: a study by small-angle X-ray scattering by Damaschun, H, Gast, K, Hahn, U, Kröber, R, Müller-Frohne, M, Zirwer, D, Damaschun, G

    Published in Biochimica et biophysica acta (18-07-1997)
    “…Small-angle X-ray scattering of RNase T1 with intact disulfide bonds was measured at 20 degrees and 60 degrees C in order to get insight into the structural…”
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  19. 19

    Acid denatured apo-cytochrome c is a random coil: evidence from small-angle X-ray scattering and dynamic light scattering by Damaschun, G, Damaschun, H, Gast, K, Gernat, C, Zirwer, D

    Published in Biochimica et biophysica acta (24-06-1991)
    “…The conformation of a denatured protein has been investigated, since the experimental data on the structure of denatured proteins have been incomplete until…”
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  20. 20

    The thermostability of natural variants of bacterial plasminogen‐activator staphylokinase by GASE, Ariane, BIRCH‐HIRSCHFELD, Eckhard, GÜHRS, Karl‐Heinz, HARTMANN, Manfred, VETTERMAN, Stefan, DAMASCHUN, Gregor, DAMASCHUN, Hilde, GAST, Klaus, MISSELWITZ, Rolf, ZIRWER, Dietrich, COLLEN, Désiré, SCHLOTT, Bernhard

    Published in European journal of biochemistry (01-07-1994)
    “…Three natural variants (wild‐type staphylokinase, [R36G, R43H]staphylokinase, and [G34S, R36G, R43H]staphylokinase) of the bacterial plasminogen‐activator…”
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