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000051328 0247_ $$2DOI$$a10.1529/biophysj.105.078980
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000051328 041__ $$aeng
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000051328 084__ $$2WoS$$aBiophysics
000051328 1001_ $$0P:(DE-Juel1)VDB58067$$aDuy, C.$$b0$$uFZJ
000051328 245__ $$aHow aggregation and conformational scrambling of unfolded states govern fluorescence emission spectra
000051328 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2006
000051328 300__ $$a3704 - 3711
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000051328 440_0 $$0882$$aBiophysical Journal$$v90$$x0006-3495
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000051328 520__ $$aIn a case study on five homologous alpha-amylases we analyzed the properties of unfolded states as obtained from treatments with GndHCl and with elevated temperatures. In particular the wavelength of the tryptophan fluorescence emission peak (lambda(max)) is a valuable parameter to characterize properties of the unfolded state. In all cases with a typical red shift of the emission spectrum occurring during structural unfolding we observed a larger magnitude of this shift for GndHCl-induced unfolding as compared to thermal unfolding. Although a quantitative relation between aggregation and reduction of the unfolding induced red shifts cannot be given, our data indicate that protein aggregation contributes significantly to smaller magnitudes of red shifts as observed during thermal unfolding. In addition, other properties of the unfolded states, most probable structural compactness or simply differences in the conformational scrambling, also affect the magnitude of red shifts. For the irreversible unfolding alpha-amylases studied here, transition temperatures and magnitudes of red shifts are strongly depending on heating rates. Lower protein concentrations and smaller heating rates lead to larger red shifts upon thermal unfolding, indicating that under these conditions the protein aggregation is less pronounced.
000051328 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
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000051328 650_2 $$2MeSH$$aDimerization
000051328 650_2 $$2MeSH$$aMultiprotein Complexes: analysis
000051328 650_2 $$2MeSH$$aMultiprotein Complexes: chemistry
000051328 650_2 $$2MeSH$$aProtein Conformation
000051328 650_2 $$2MeSH$$aProtein Denaturation
000051328 650_2 $$2MeSH$$aProtein Folding
000051328 650_2 $$2MeSH$$aSpectrometry, Fluorescence: methods
000051328 650_2 $$2MeSH$$aStructure-Activity Relationship
000051328 650_2 $$2MeSH$$aTemperature
000051328 650_2 $$2MeSH$$aalpha-Amylases: analysis
000051328 650_2 $$2MeSH$$aalpha-Amylases: chemistry
000051328 650_7 $$00$$2NLM Chemicals$$aMultiprotein Complexes
000051328 650_7 $$0EC 3.2.1.1$$2NLM Chemicals$$aalpha-Amylases
000051328 650_7 $$2WoSType$$aJ
000051328 7001_ $$0P:(DE-Juel1)131961$$aFitter, J.$$b1$$uFZJ
000051328 773__ $$0PERI:(DE-600)1477214-0$$a10.1529/biophysj.105.078980$$gVol. 90, p. 3704 - 3711$$p3704 - 3711$$q90<3704 - 3711$$tBiophysical journal$$v90$$x0006-3495$$y2006
000051328 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1440751
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