Search Results - "Damaschun, Hilde"

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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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  3. 3

    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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  4. 4

    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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    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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    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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    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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    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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    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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    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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    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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    Physical and conformational properties of staphylokinase in solution by Damaschun, G, Damaschun, H, Gast, K, Misselwitz, R, Zirwer, D, Gührs, K H, Hartmann, M, Schlott, B, Triebel, H, Behnke, D

    Published in Biochimica et biophysica acta (13-02-1993)
    “…The structure of staphylokinase has been analyzed by solution X-ray scattering, dynamic light scattering, ultracentrifugation and ultraviolet circular…”
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    Spermine-DNA complexes build up metastable structures. Small-angle X-ray scattering and circular dichroism studies by Becker, M., Misselwitz, R., Damaschun, Hilde, Damaschun, G., Zirwer, D.

    Published in Nucleic acids research (10-11-1979)
    “…Spermine-DNA complexes have been examined by small-angle and wide-angle X-ray scattering as well as by circular dichroism studies. Condensed complexes are…”
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    Study of DNA-spermine interactions by use of small-angle and wide-angle X-ray scattering and circular dichroism by Damaschun, Hilde, Damaschun, G., Becker, M., Buder, E., Misselwitz, R., Zirwer, D.

    Published in Nucleic acids research (01-10-1978)
    “…Circular dichroism measurements with DNA-spermine complexes at 0.075 M NaCl and at 0.15 M NaCl reveal +Ψ (type I) and −Ψ (type II) CD spectra respectively…”
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    Conformation of thermally denatured RNase T1 with intact disulfide bonds: A study by small-angle X-ray scattering by Damaschun, Hilde, Gast, Klaus, Hahn, Ulrich, Kröber, Reinhard, Müller-Frohne, Marlies, Zirwer, Dietrich, Damaschun, Gregor

    “…Small-angle X-ray scattering of RNase T1 with intact disulfide bonds was measured at 20° and 60°C in order to get insight into the structural changes of the…”
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