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pro vyhledávání: '"Andreas W. E. Dilg"'
Autor:
Andreas W. E. Dilg, Fritz G. Parak, Claudio Luchinat, Francesco Capozzi, O. Iakovleva, Ivano Bertini, Matthias Mentler
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 6:232-246
Mossbauer, 57Fe ENDOR, CW and pulsed EPR experiments were performed on the reduced and the oxidized high-potential iron proteins (HiPIPs) of the wild type (WT) and the C77S mutant from Chromatium vinosum. The EPR spectra of the oxidized WT and mutant
Autor:
O. Iakovleva, Klaus Achterhold, Giovanna Mincione, Ivano Bertini, Matthias Mentler, Fritz G. Parak, Claudio Luchinat, Andreas W. E. Dilg
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 4:727-741
Mössbauer spectra of the oxidized [Fe4S4]3+ and the reduced [Fe4S4]2+ clusters in the high-potential iron protein I from Ectothiorhodospira halophila were measured in a temperature range from 5 K to 240 K. EPR measurements and 57Fe electron-nuclear
Structural Relaxation from X- ray irradiated metastable Hbmet investigated by Mössbauer Spectroscopy
Autor:
Andreas W. E. Dilg, Fritz G. Parak, Niklas Engler, O. Iakovleva, Valeri E. Prusakov, I. Ortalli, S. Croci
Publikováno v:
Hyperfine Interactions (C) ISBN: 9781402010873
Protein functions are strictly connected to their structural dynamics. Actually, the study of haemoglobin metastable states is a useful way to have insight in to structural changes that lead the protein from one stable state to another. Mossbauer spe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a4c9f3878ab4f8c67135ca06b921b92
https://doi.org/10.1007/978-94-010-0281-3_59
https://doi.org/10.1007/978-94-010-0281-3_59
Autor:
Andreas W. E. Dilg, O. Iakovleva, Francesco Capozzi, Claudio Luchinat, Wolfram Meyer-Klaucke, Elena Babini, Klaus Grantner, Ivano Bertini, Fritz G. Parak
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 7(7-8)
The temperature dependence of the mean square displacement of the (57)Fe nuclei due to motion faster than 100 ns are measured by temperature-dependent Mossbauer spectroscopy for oxidized and reduced HiPIPs from Ectothiorhodospira halophila, Chromatiu