| Home > Publications database > Amyloid-Like Structures Formed by Azobenzene Peptides: Light-Triggered Disassembly > print |
| 001 | 22704 | ||
| 005 | 20240619092043.0 | ||
| 024 | 7 | _ | |2 DOI |a 10.1155/2012/108959 |
| 024 | 7 | _ | |2 WOS |a WOS:000306505500016 |
| 024 | 7 | _ | |2 ISSN |a 0887-6703 |
| 024 | 7 | _ | |2 MLZ |a Deeg:22704 |
| 037 | _ | _ | |a PreJuSER-22704 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 530 |
| 084 | _ | _ | |2 WoS |a Biochemical Research Methods |
| 084 | _ | _ | |2 WoS |a Spectroscopy |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Deeg, A.A. |b 0 |
| 245 | _ | _ | |a Amyloid-Like Structures Formed by Azobenzene Peptides: Light-Triggered Disassembly |
| 260 | _ | _ | |a Springfield, Or. |b Aster Pub. Corp. |c 2012 |
| 300 | _ | _ | |a 387 - 391 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 8881 |a Spectroscopy |v 27 |x 0887-6703 |y 5-6 |
| 500 | _ | _ | |a The work was supported by the German Science Foundation, SFB 749, and the Munich Center of Integrated Protein Science, CIPSM. The University of Zurich did not contribute to this work. |
| 520 | _ | _ | |a The light-driven disassembly process of amyloid-like structures formed by azobenzene model peptides is studied by time-resolved mid-IR spectroscopy from nanoseconds to minutes. The investigated peptide consists of two amino acid strands connected by the azobenzene switch. The peptides aggregate to amyloid-like structures when the azobenzene chromophore is in the trans-conformation. Illumination, resulting in a trans-to cis-isomerization of the azobenzene, leads to disaggregation of the aggregated structures. After optical excitation and isomerization of the azobenzene, one finds absorption changes which recover to a large extent on the time scale of few nanoseconds. These early absorption transients are assigned to the relaxation of vibrational excess energy (heat) or to structural rearrangements of isomerized azobenzene and the aggregated surroundings. It is only on the time scale of minutes that spectral signatures appear which are characteristic for the disassembly of the aggregated structure. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK505 |2 G:(DE-HGF) |x 0 |c FUEK505 |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (FUEK505) |
| 536 | _ | _ | |0 G:(DE-HGF)POF2-544 |a 544 - In-house Research with PNI (POF2-544) |c POF2-544 |f POF II |x 1 |
| 588 | _ | _ | |a Dataset connected to Web of Science |
| 650 | _ | 7 | |2 WoSType |a J |
| 650 | 2 | 7 | |0 V:(DE-MLZ)SciArea-110 |2 V:(DE-HGF) |a Chemistry |x 0 |
| 650 | 1 | 7 | |a Polymers, Soft Nano Particles and Proteins |0 V:(DE-MLZ)GC-1602-2016 |2 V:(DE-HGF) |x 1 |
| 650 | 1 | 7 | |a Key Technologies |0 V:(DE-MLZ)GC-150-1 |2 V:(DE-HGF) |x 0 |
| 653 | 2 | 0 | |2 Author |a Peptides |
| 653 | 2 | 0 | |2 Author |a amyloid-disassembly |
| 653 | 2 | 0 | |2 Author |a azobenzene |
| 653 | 2 | 0 | |2 Author |a nanostructures |
| 653 | 2 | 0 | |2 Author |a time-resolved-vibrational spectroscopy |
| 693 | _ | _ | |0 EXP:(DE-MLZ)External-20140101 |5 EXP:(DE-MLZ)External-20140101 |e External Measurement |x 0 |
| 700 | 1 | _ | |0 P:(DE-Juel1)138266 |a Schrader, T.E. |b 1 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Strzalka, H. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Pfizer, J. |b 3 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Moroder, L. |b 4 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Zinth, W. |b 5 |
| 773 | _ | _ | |0 PERI:(DE-600)2068779-5 |a 10.1155/2012/108959 |g Vol. 27, p. 387 - 391 |p 387 - 391 |q 27<387 - 391 |t Spectroscopy: An International Journal |v 27 |x 0887-6703 |y 2012 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1155/2012/108959 |
| 909 | C | O | |o oai:juser.fz-juelich.de:22704 |p VDB:MLZ |p VDB |
| 913 | 2 | _ | |0 G:(DE-HGF)POF3-623 |1 G:(DE-HGF)POF3-620 |2 G:(DE-HGF)POF3-600 |a DE-HGF |b Forschungsbereich Materie |l In-house research on the structure, dynamics and function of matter |v Neutrons for Research on Condensed Matter |x 0 |
| 913 | 1 | _ | |x 0 |v In-house Research with PNI |1 G:(DE-HGF)POF2-540 |0 G:(DE-HGF)POF2-544 |2 G:(DE-HGF)POF2-500 |a DE-HGF |b Struktur der Materie |4 G:(DE-HGF)POF |3 G:(DE-HGF)POF2 |l Forschung mit Photonen, Neutronen, Ionen |
| 914 | 1 | _ | |y 2012 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |2 StatID |a JCR/ISI refereed |
| 915 | _ | _ | |0 StatID:(DE-HGF)0100 |2 StatID |a JCR |
| 915 | _ | _ | |0 StatID:(DE-HGF)0110 |2 StatID |a WoS |b Science Citation Index |
| 915 | _ | _ | |0 StatID:(DE-HGF)0111 |2 StatID |a WoS |b Science Citation Index Expanded |
| 915 | _ | _ | |0 StatID:(DE-HGF)0150 |2 StatID |a DBCoverage |b Web of Science Core Collection |
| 915 | _ | _ | |0 StatID:(DE-HGF)0199 |2 StatID |a DBCoverage |b Thomson Reuters Master Journal List |
| 915 | _ | _ | |0 StatID:(DE-HGF)1020 |2 StatID |a DBCoverage |b Current Contents - Social and Behavioral Sciences |
| 920 | 1 | _ | |0 I:(DE-Juel1)ICS-1-20110106 |g ICS |k ICS-1 |l Neutronenstreuung |x 0 |
| 920 | 1 | _ | |0 I:(DE-Juel1)JCNS-FRM-II-20110218 |k JCNS (München) ; Jülich Centre for Neutron Science JCNS (München) ; JCNS-FRM-II |l JCNS-FRM-II |x 1 |
| 920 | 1 | _ | |0 I:(DE-Juel1)JCNS-1-20110106 |g JCNS |k JCNS-1 |l Neutronenstreuung |x 2 |
| 970 | _ | _ | |a VDB:(DE-Juel1)139412 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-1-20110106 |
| 980 | _ | _ | |a I:(DE-Juel1)JCNS-FRM-II-20110218 |
| 980 | _ | _ | |a I:(DE-Juel1)JCNS-1-20110106 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-8-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)JCNS-1-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)JCNS-FRM-II-20110218 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|