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000038378 0247_ $$2pmid$$apmid:15170487
000038378 0247_ $$2DOI$$a10.1039/b400976b
000038378 0247_ $$2WOS$$aWOS:000221746800012
000038378 037__ $$aPreJuSER-38378
000038378 041__ $$aeng
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000038378 084__ $$2WoS$$aBiochemistry & Molecular Biology
000038378 084__ $$2WoS$$aBiophysics
000038378 084__ $$2WoS$$aChemistry, Physical
000038378 1001_ $$0P:(DE-Juel1)VDB37437$$aBednarz, T.$$b0$$uFZJ
000038378 245__ $$aFunctional variations among LOV domains as revealed by FTIR difference spectroscopy
000038378 260__ $$aCambridge$$bRoyal Society of Chemistry$$c2004
000038378 300__ $$a575 - 579
000038378 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000038378 440_0 $$09703$$aPhotochemical and Photobiological Sciences$$v3$$x1474-905X
000038378 500__ $$aRecord converted from VDB: 12.11.2012
000038378 520__ $$aThe two LOV domains, LOV1 and LOV2, from Chlamydomonas reinhardtii were investigated by light-induced FT-IR difference spectroscopy and compared to the LOV domain of Bacillus subtilis (YtvA-LOV). It is shown that the two S-H conformations of the reactive LOV1 cysteine C57(1) are exposed to environments of different hydrogen bonding strength. Thus, the two rotamer configurations of C57 might be related to the fact that the triplet state decays bi-exponentially into the LOV1-390 photoproduct. Exchange of the two other cysteines of LOV1 (C32S and C83S) does not alter the S-H stretching band providing evidence that this band feature arises solely from C57. The reactive cysteine of LOV2 from Chlamydomonas reinhardtii (C250) and of YtvA-LOV (C62) exhibit both a homogenous S-H stretching vibrational band which suggests a single conformer of the amino acid side chain. Finally, the FT-IR difference spectrum of YtvA from Bacillus subtilis comprising the light absorbing LOV domain and the putative signaling STAS (sulfate transporter/antisigma-factor antagonist) domain, reveals conformational changes in the latter after blue-light excitation.
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000038378 588__ $$aDataset connected to Web of Science, Pubmed
000038378 650_2 $$2MeSH$$aAnimals
000038378 650_2 $$2MeSH$$aBacillus subtilis: physiology
000038378 650_2 $$2MeSH$$aBacillus subtilis: radiation effects
000038378 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000038378 650_2 $$2MeSH$$aBacterial Proteins: genetics
000038378 650_2 $$2MeSH$$aBacterial Proteins: physiology
000038378 650_2 $$2MeSH$$aChlamydomonas reinhardtii: physiology
000038378 650_2 $$2MeSH$$aChlamydomonas reinhardtii: radiation effects
000038378 650_2 $$2MeSH$$aCrystallography, X-Ray
000038378 650_2 $$2MeSH$$aProtein Conformation
000038378 650_2 $$2MeSH$$aSpectrometry, Fluorescence
000038378 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared: methods
000038378 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000038378 650_7 $$2WoSType$$aJ
000038378 7001_ $$0P:(DE-HGF)0$$aLosi, A.$$b1
000038378 7001_ $$0P:(DE-HGF)0$$aGärtner, W.$$b2
000038378 7001_ $$0P:(DE-HGF)0$$aHegemann, P.$$b3
000038378 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b4$$uFZJ
000038378 773__ $$0PERI:(DE-600)2072584-X$$a10.1039/b400976b$$gVol. 3, p. 575 - 579$$p575 - 579$$q3<575 - 579$$tPhotochemical & photobiological sciences$$v3$$x1474-905X$$y2004
000038378 8567_ $$uhttp://dx.doi.org/10.1039/b400976b
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000038378 9131_ $$0G:(DE-Juel1)FUEK255$$bLeben$$kL01$$lFunktion und Dysfunktion des Nervensystems$$vNeurowissenschaften$$x0
000038378 9141_ $$y2004
000038378 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000038378 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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000038378 980__ $$aI:(DE-Juel1)ICS-6-20110106
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