Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Inge Heise"'
Autor:
Inge Heise
Publikováno v:
MedieKultur: Journal of Media and Communication Research, Vol 3, Iss 6 (1987)
Externí odkaz:
https://doaj.org/article/18ea28b9b9724bf6862c5a2a7ef6d2f4
Autor:
Friedrich Siebert, Wolfgang Gärtner, Francisco Velazquez Escobar, Żaneta Nogacz, Ronald González, Maria Andrea Mroginski, Patrick Piwowarski, Patrick Scheerer, Peter Hildebrandt, Anh Duc Nguyen, Norbert Michael, Franz Bartl, Inge Heise, Maria Fernandez Lopez
Publikováno v:
Biochemistry. 58(33)
Bacteriophytochromes harboring a biliverdin IXα (BV) chromophore undergo photoinduced reaction cascades to switch between physiologically inactive and active states. Employing vibrational spectroscopic and computational methods, we analyzed the role
Autor:
Markus Knipp, Elena Decaneto, Stefania Abbruzzetti, Cristiano Viappiani, Inge Heise, Wolfgang Lubitz
Publikováno v:
Photochemical & photobiological sciences
14 (2015): 300–307. doi:10.1039/c4pp00297k
info:cnr-pdr/source/autori:Decaneto E.; Abbruzzetti S.; Heise I.; Lubitz W.; Viappiani C.; Knipp M./titolo:A caged substrate peptide for matrix metalloproteinases/doi:10.1039%2Fc4pp00297k/rivista:Photochemical & photobiological sciences (Print)/anno:2015/pagina_da:300/pagina_a:307/intervallo_pagine:300–307/volume:14
14 (2015): 300–307. doi:10.1039/c4pp00297k
info:cnr-pdr/source/autori:Decaneto E.; Abbruzzetti S.; Heise I.; Lubitz W.; Viappiani C.; Knipp M./titolo:A caged substrate peptide for matrix metalloproteinases/doi:10.1039%2Fc4pp00297k/rivista:Photochemical & photobiological sciences (Print)/anno:2015/pagina_da:300/pagina_a:307/intervallo_pagine:300–307/volume:14
Based on the widely applied fluorogenic peptide FS-6 (Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2; Mca = methoxycoumarin-4-acetyl; Dpa = N-3-(2,4-dinitrophenyl)l-α,β-diaminopropionyl) a caged substrate peptide Ac-Lys-Pro-Leu-Gly-Lys*-Lys-Ala-Arg-NH2 (*
Publikováno v:
Photochemistry and Photobiology. 87:1031-1035
The photoinduced conversion via the aci-nitro into the nitroso form was studied for 4,5-dimethoxy-2-nitrobenzyl alcohols attached to various leaving groups: amino acids histidine (NHis) and aspartate (NAsp) as well as their fluorenylmethoxycarbonyl d