Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Ruth Hielscher"'
Autor:
Thorsten Friedrich, Petra Hellwig, Mariana Voicescu, Emmanuel Gnandt, Ruth Hielscher, Michelle Yegres
Publikováno v:
Biochemistry
Biochemistry, 2013, 52 (50), pp.8993-9000. ⟨10.1021/bi4009903⟩
Biochemistry, 2013, 52 (50), pp.8993-9000. ⟨10.1021/bi4009903⟩
PMID: 24279322; The NADH:ubiquinone oxidoreductase (complex I) couples the transfer of electrons from NADH to ubiquinone with the translocation of protons across the membrane. It was proposed that the electron transfer involves quinoid groups localiz
Publikováno v:
Vibrational Spectroscopy. 55:258-266
In this work we analyzed the specificity of the amide VI band for different types of secondary structure elements in protein structures. This band involves the bending motion of the C O group of the peptide chain that is typically observed in the spe
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1787(6):609-616
Specific protein-lipid interactions have been identified in X-ray structures of membrane proteins. The role of specifically bound lipid molecules in protein function remains elusive. In the current study, we investigated how phospholipids influence c
Autor:
Thorsten Friedrich, Daniel Schneider, Ruth Hielscher, Markus Kohlstädt, Thomas Pohl, Katerina Dörner, Petra Hellwig, Bettina Böttcher, Stefan Stolpe
Publikováno v:
Biochemical Society Transactions. 36:971-975
The energy-converting NADH:ubiquinone oxidoreductase, also known as respiratory complex I, couples the transfer of electrons from NADH to ubiquinone with the translocation of protons across the membrane. Electron microscopy revealed the two-part stru
Publikováno v:
Protein Expression and Purification. 56:279-285
Folding and assembly studies with alpha-helical membrane proteins are often hampered by the absence of high-level expression systems as well as by missing suitable in vitro refolding procedures. Experimental constraints and requirements for heterolog
Autor:
Ruth Hielscher, Jie Zhang, Robert B. Gennis, James Hemp, Petra Hellwig, Hideto Miyoshi, Jeffrey P. Osborne, Ke Yang, Ahmet S. Vakkasoglu
Publikováno v:
Biochemistry. 46:3270-3278
Cytochrome bd is a quinol oxidase from Escherichia coli, which is optimally expressed under microaerophilic growth conditions. The enzyme catalyzes the two-electron oxidation of either ubiquinol or menaquinol in the membrane and scavenges O2 at low c
Autor:
Ruth Hielscher, Petra Hellwig
Publikováno v:
Spectroscopy: An International Journal.
We describe the specific spectral signature of different phospholipids and sphingolipids in the far infrared. Three specific spectral domains have been found: the head group contributions (600 and 480 cm−1); the modes of the torsion motion of the h
Publikováno v:
35th International Conference on Infrared, Millimeter, and Terahertz Waves.
The use of the far IR spectral range presents a novel approach for analysis of proteins. Here it is presented for the analysis of Fe-S vibrations (500–200 cm−1) and of the intra-and intermolecular H-bonding signature (300–50 cm−1) in Rieske p
Publikováno v:
ChemPhysChem
ChemPhysChem, 2011, 12 (1), pp.217-224. ⟨10.1002/cphc.201000688⟩
ChemPhysChem, 2011, 12 (1), pp.217-224. ⟨10.1002/cphc.201000688⟩
PMID: 21226204; The catalytic activity of the respiratory NADH:ubiquinone oxidoreductase (complex I) is based on conformational reorganizations. Herein we probe the effect of substrates on the conformational flexibility of complex I by means of (1)H/
Autor:
Ruth Hielscher, Petra Hellwig
Publikováno v:
Chemphyschem : a European journal of chemical physics and physical chemistry. 11(2)
Phospholipids are studied by means of Fourier transform infrared (FTIR) spectroscopy in the mid- and far-infrared spectral ranges, thereby establishing the hydrogen-bonding continuum as a function of the temperature. The well-known mid-infrared spect