Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Hilde Damaschun"'
Publikováno v:
Journal of Molecular Biology. 291:715-725
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 environment. The great influence of the latter interactions is demonstrated for the enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc31e8849853e1d86c8cc7a6c6319dad
https://doi.org/10.1006/jmbi.1999.3009
https://doi.org/10.1006/jmbi.1999.3009
Autor:
Marlies Müller-Frohne, Hilde Damaschun, Klaus Gast, K Eckert, Dietrich Zirwer, Gregor Damaschun, H R Maurer, J Czarnecki, K Schulze-Forster
Publikováno v:
Biochemistry. 34:13211-13218
Prothymosin is an acidic protein with an unusual amino acid composition. Though its exact function is not yet known, its high evolutionary conservation and wide tissue distribution suggest an essential biological role. Its physical state, which is co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::313585e5bdbd0f6465ee7c6c193ab6bf
https://doi.org/10.1021/bi00040a037
https://doi.org/10.1021/bi00040a037
Autor:
Gregor Damaschun, Stefan Vetterman, Karl-Heinz Gührs, Klaus Gast, Dietrich Zirwer, Rolf Misselwitz, Bernhard Schlott, Hilde Damaschun, Manfred Hartmann, Desire Collen, Ariane Gase, Eckhard Birch-Hirschfeld
Publikováno v:
European Journal of Biochemistry. 223:303-308
Three natural variants (wild-type staphylokinase, [R36G, R43H]staphylokinase, and [G34S, R36G, R43H]staphylokinase) of the bacterial plasminogen-activator staphylokinase, a 136-amino-acid protein secreted by certain Staphylococcus aureus strains, hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dfe384ba735802717e572e9f6c3be46
https://doi.org/10.1111/j.1432-1033.1994.tb18995.x
https://doi.org/10.1111/j.1432-1033.1994.tb18995.x
Publikováno v:
Biochemistry. 32:7747-7752
Under mildly destabilizing conditions (0.7 M GuHCl), phosphoglycerate kinase from yeast undergoes a reversible two-step equilibrium unfolding transition when the temperature is lowered from 30 to 1 degree C (Griko, Y. V., Venyaminov, S. Y., & Privalo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5091819deb55d9e1aeb918e538a7ac0
https://doi.org/10.1021/bi00081a020
https://doi.org/10.1021/bi00081a020
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1078:289-295
The conformation of a denatured protein has been investigated, since the experimental data on the structure of denatured proteins have been incomplete until now. The Stokes' radius Rs and the radius of gyration Rg of apo-cytochrome c at pH 2.3 have b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca0b7350fd22bc83f1b26827b85beb8e
https://doi.org/10.1016/0167-4838(91)90571-g
https://doi.org/10.1016/0167-4838(91)90571-g
Autor:
A. J. Modler, Hilde Damaschun, Reinhard Krober, Klaus Gast, R. Golbik, Dietrich Zirwer, Gudrun Lutsch, Gregor Damaschun
Publikováno v:
European biophysics journal : EBJ. 32(8)
The dependence on environmental conditions of the assembly of barstar into amyloid fibrils was investigated starting from the nonnative, partially folded state at low pH (A-state). The kinetics of this process was monitored by CD spectroscopy and sta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24ade9183d92a8e91b3451b80f2c92b4
https://pubmed.ncbi.nlm.nih.gov/12898068
https://pubmed.ncbi.nlm.nih.gov/12898068
Autor:
Dietrich Zirwer, Hilde Damaschun, Martin Wieske, Heinz Fabian, Klaus Gast, Gregor Damaschun, Reinhard Krober
Publikováno v:
Proteins. 39(3)
Yeast phosphoglycerate kinase is a structurally well-characterized enzyme consisting of 415 amino acids without disulfide bonds. Anion-induced refolding from its acid-unfolded state gives rise to the formation of worm-like amyloid fibrils with a pers
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6060f5435571c6980ce462669808f34
https://pubmed.ncbi.nlm.nih.gov/10737941
https://pubmed.ncbi.nlm.nih.gov/10737941
Autor:
Dietrich Zirwer, Klaus Gast, Hilde Damaschun, Marlies Müller-Frohne, Ulrich Hahn, Gregor Damaschun, Matthias Wirth
Publikováno v:
FEBS letters. 403(3)
Ribonuclease T1 can be unfolded and refolded without forming noticeable amounts of aggregates allowing to characterise the dimensions of a protein in different denatured states in terms of the Stokes radius R S . Upon thermal unfolding R S increases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7579d49c97e98230f811d9db95d115a5
https://pubmed.ncbi.nlm.nih.gov/9091310
https://pubmed.ncbi.nlm.nih.gov/9091310
Autor:
Klaus Gast, Wolfgang Pfeil, Hilde Damaschun, Dietrich Zirwer, Rolf Misselwitz, Gregor Damaschun, J. J. Müller
Publikováno v:
Biochemistry. 32(30)
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 dynamic light scattering, small-angle X-ray scattering, differential scanning calorimetry,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d39b3f9494b7beac2ef003d226f209d7
https://pubmed.ncbi.nlm.nih.gov/8347582
https://pubmed.ncbi.nlm.nih.gov/8347582
Autor:
Klaus Gast, Dietrich Zirwer, Bernhard Schlott, Karl-Heinz Gührs, Hilde Damaschun, Hans Triebel, Detlev Behnke, Gregor Damaschun, Rolf Misselwitz, Manfred Hartmann
Publikováno v:
Biochimica et biophysica acta. 1161(2-3)
The structure of staphylokinase has been analyzed by solution X-ray scattering, dynamic light scattering, ultracentrifugation and ultraviolet circular dichroism spectroscopy. Staphylokinase has a radius of gyration of 2.3 nm, a Stokes radius of 2.12
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cae54818b9932528e9388fce5f65b1d5
https://pubmed.ncbi.nlm.nih.gov/8431473
https://pubmed.ncbi.nlm.nih.gov/8431473