Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Hans Juergen Hinz"'
Autor:
Hans-Jürgen Hinz
The strong trend in the Biological Sciences towards a quantitative characterization of processes has promoted an increased use of thermo dynamic reasoning. This development arises not only from the well known power of thermodynamics to predict th
Autor:
Mike Kokkinidis, Josef Flossdorf, Peter Weber, Hans Juergen Hinz, Gianni Cesareni, Christian Steif
Publikováno v:
Biochemistry. 32(15)
Detailed thermodynamic and spectroscopic studies were carried out on the ColE1-ROP protein in order to establish a quantitative basis for the contribution of noncovalent interactions to the stability of four-helix-bundle proteins. The energetics of b
Autor:
Ulrich Hahn, Hans Juergen Hinz, Rainer Quaas, Michael Renner, Franz X. Schmid, Thomas Kiefhaber
Publikováno v:
Biochemistry. 29(36)
The conformational stability of recombinant Lys25-ribonuclease T1 has been determined by differential scanning microcalorimetry (DSC), UV-monitored thermal denaturation measurements, and isothermal Gdn.HCl unfolding studies. Although rather different
Publikováno v:
Biochemistry. 26:3544-3551
Gibbs energy, enthalpy, and entropy data were determined for two selectively modified analogues of bovine pancreatic trypsin inhibitor (BPTI) to provide a model free set of thermodynamic parameters that characterize (a) the energetic and entropic con
Publikováno v:
Biochemistry. 18(10)
Association of the apo-beta 2 and the holo-(beta-PLP)2 subunits of tryptophan synthase from Escherichia coli (L-serine hydro-lyase (adding indole) (EC 4.2.1.20)) with alpha subunits of the same enzyme has been studied by microcalorimetry. The results
Autor:
Heinrich Wiesinger, Hans Juergen Hinz
Publikováno v:
Biochemistry. 23(21)
The binding of indole and L-serine to the isolated alpha and beta 2 subunits and the native alpha 2 beta 2 complex of tryptophan synthase from Escherichia coli was investigated by direct microcalorimetry to reveal the energetic adaptation of ligand b
Autor:
Hans Juergen Hinz, Heinrich Wiesinger
Publikováno v:
Biochemistry. 23(21)
The energetics of binding of the coenzyme pyridoxal 5'-phosphate (PLP) to both the apo beta 2 subunit and the apo alpha 2 beta 2 complex of tryptophan synthase from Escherichia coli has been investigated as a function of pH and temperature by direct
Publikováno v:
Biochemistry. 19(14)
Fluorescence, equilibrium dialysis, and microcalorimetric measurements have been performed on complex formation between pig heart muscle lactate dehydrogenase (EC 1.1.1.27) and a series of systematically modified nicotinamide adenine dinucleotide ana
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