Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Ionela Radu"'
Publikováno v:
Hyperion Economic Journal, Vol 2, Iss 1, Pp 46-49 (2014)
According to international auditing standards, fraud is an intentionally action realised by one or more persons as management, employees or third parties, action that generate erroneous interpretation of financial statements. The real intention is to
Externí odkaz:
https://doaj.org/article/a7f6763603e34d16b4d4c77874e0574b
Autor:
Young Jun Kim, Georg Büldt, Torben Hoomann, Jörg Labahn, Ivan L. Budyak, Ionela Radu, Joachim Heberle, Martin Engelhard, Ramona Schlesinger
Publikováno v:
Biophysical Chemistry. 150:23-28
Sensory rhodopsin I (SRI) from Halobacterium salinarum mediates both positive and negative phototaxis in a light-dependent manner. SRI photoactivation elicits extensive structural changes which are transmitted to the cognate transducer (HtrI). The at
Autor:
Gabriele Fischer von Mollard, Joachim Heberle, Christian Bamann, Ionela Radu, Melanie Nack, Ernst Bamberg, Michael Gossing
Publikováno v:
Photochemical & Photobiological Sciences. 9:194-198
The light-gated cation channel Channelrhodopsin-2 (ChR2), a retinylidene protein found in the eye-spot of Chlamydomonas reinhardtii, became an optogenetic tool to trigger neurophysiological responses by light and, thus, revolutionized spatio-temporal
Publikováno v:
Journal of Polymer Science Part A: Polymer Chemistry. 36:1615-1623
Unsaturated macromolecular carboxybetaines were obtained by reaction of poly(4-vinylpyridine) and poly(N-vinylimidazole) with propiolic acid. A kinetic model was presented for 4-methylpyridine. It consists of three coupled reactions: neutralization,
Autor:
Karsten Neumann, Joachim Heberle, Mirka-Kristin Neumann-Verhoefen, Josef Wachtveitl, Ionela Radu, Ernst Bamberg, Christian Bamann
Publikováno v:
Journal of the American Chemical Society. 135(18)
The primary reaction dynamics of channelrhodopsin-2 was investigated using femtosecond vis-pump/mid-IR probe spectroscopy. Due to the fast deactivation of the excited state in channelrhodopsin-2, it is possible to observe the direct impact of retinal
Autor:
Tom Resler, Cristiano Viappiani, Christian Bamann, Ernst Bamberg, Stefania Abbruzzetti, Bernd-Joachim Schultz, Ramona Schlesinger, Ana-Nicoleta Bondar, Coral del Val, Melanie Nack, Ionela Radu, Joachim Heberle
Electrophysiological experiments showed that the light-activated cation channel channelrhodopsin-2 (ChR2) pumps protons in the absence of a membrane potential. We determined here the kinetics of transient pH change using a water-soluble pH-indicator.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0409f417f14c1fb37b2b558f768a1598
https://refubium.fu-berlin.de/handle/fub188/16160
https://refubium.fu-berlin.de/handle/fub188/16160
Publikováno v:
ChemInform. 42
Time-resolved Fourier transform infrared spectroscopy (FT-IR) offers distinct advantages concerning restrictions pertinent to biomolecules. In particular, it is possible to monitor the temporal evolution of the reaction mechanism of complex machineri
Autor:
Joachim Heberle, Ramona Schlesinger, Ionela Radu, Christian Bamann, Ernst Bamberg, Melanie Nack
Publikováno v:
ResearcherID
The light-gated cation channel Channelrhodopsin-2 (ChR2), a retinylidene protein found in the eye-spot of Chlamydomonas reinhardtii, became an optogenetic tool to trigger neurophysiological responses by light and, thus, revolutionized spatio-temporal
Publikováno v:
Supramolecular Structure and Function 10 ISBN: 9789400708921
Time-resolved Fourier transform infrared spectroscopy (FT-IR) has been proven to be an excellent method with important applications in bioscience. In particular, it is possible to monitor the temporal evolution of the reaction mechanism of complex ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0ddacc017b711b4de68ffc38d9a0891e
https://doi.org/10.1007/978-94-007-0893-8_2
https://doi.org/10.1007/978-94-007-0893-8_2
The introduction of time-resolved Fourier transform infrared (FT-IR) spectroscopy to biochemistry opened the possibility of monitoring the catalytic mechanism of proteins along their reaction pathways. The infrared approach is very fruitful, particul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::987add7e9d6bb86e653dea714504ecf9
https://publica.fraunhofer.de/handle/publica/220013
https://publica.fraunhofer.de/handle/publica/220013