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000051048 084__ $$2WoS$$aBiochemistry & Molecular Biology
000051048 1001_ $$0P:(DE-HGF)0$$aPolverini, E.$$b0
000051048 245__ $$aMolten globule formation in apomyoglobin monitored by the fluorescent probe nile red
000051048 260__ $$aColumbus, Ohio$$bAmerican Chemical Society$$c2006
000051048 300__ $$a5111 - 5121
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000051048 440_0 $$0798$$aBiochemistry$$v45$$x0006-2960
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000051048 520__ $$aThe interaction of nile red (NR) with apomyoglobin (ApoMb) in the native (pH 7) and molten globule (pH 4) states was investigated using experimental and computational methods. NR binds to hydrophobic locations in ApoMb with higher affinity (K(d) = 25 +/- 5 microM) in the native state than in the molten globule state (K(d) = 52 +/- 5 microM). In the molten globule state, NR is located in a more hydrophobic environment. The dye does not bind to the holoprotein, suggesting that the binding site is located at the heme pocket. In addition to monitoring steady-state properties, the fluorescence emission of NR is capable of tracking submillisecond, time-resolved structural rearrangements of the protein, induced by a nanosecond pH jump. Molecular dynamics simulations were run on ApoMb at neutral pH and at pH 4. The structure obtained for the molten globule state is consistent with the experimentally available structural data. The docking of NR with the crystal structure shows that the ligand binds into the binding pocket of the heme group, with an orientation bringing the planar ring system of NR to overlap with the position of two of the heme porphyrin rings in Mb. The docking of NR with the ApoMb structure at pH 4 shows that the dye binds to the heme pocket with a slightly less favorable binding energy, in keeping with the experimental K(d) value. Under these conditions, NR is positioned in a different orientation, reaching a more hydrophobic environment in agreement with the spectroscopic data.
000051048 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000051048 588__ $$aDataset connected to Web of Science, Pubmed
000051048 650_2 $$2MeSH$$aAnimals
000051048 650_2 $$2MeSH$$aApoproteins: chemistry
000051048 650_2 $$2MeSH$$aApoproteins: metabolism
000051048 650_2 $$2MeSH$$aBinding Sites
000051048 650_2 $$2MeSH$$aComputer Simulation
000051048 650_2 $$2MeSH$$aFluorescent Dyes: analysis
000051048 650_2 $$2MeSH$$aHorses
000051048 650_2 $$2MeSH$$aHydrogen-Ion Concentration
000051048 650_2 $$2MeSH$$aModels, Molecular
000051048 650_2 $$2MeSH$$aMyoglobin: chemistry
000051048 650_2 $$2MeSH$$aMyoglobin: metabolism
000051048 650_2 $$2MeSH$$aOxazines: analysis
000051048 650_2 $$2MeSH$$aOxazines: chemistry
000051048 650_2 $$2MeSH$$aProtein Binding
000051048 650_2 $$2MeSH$$aProtein Folding
000051048 650_2 $$2MeSH$$aProtein Structure, Tertiary
000051048 650_7 $$00$$2NLM Chemicals$$aApoproteins
000051048 650_7 $$00$$2NLM Chemicals$$aFluorescent Dyes
000051048 650_7 $$00$$2NLM Chemicals$$aMyoglobin
000051048 650_7 $$00$$2NLM Chemicals$$aOxazines
000051048 650_7 $$00$$2NLM Chemicals$$aapomyoglobin
000051048 650_7 $$07385-67-3$$2NLM Chemicals$$anile red
000051048 650_7 $$2WoSType$$aJ
000051048 7001_ $$0P:(DE-HGF)0$$aCugini, G.$$b1
000051048 7001_ $$0P:(DE-HGF)0$$aAnnoni, F.$$b2
000051048 7001_ $$0P:(DE-HGF)0$$aAbbruzzetti, S.$$b3
000051048 7001_ $$0P:(DE-HGF)0$$aViappiani, C.$$b4
000051048 7001_ $$0P:(DE-Juel1)131924$$aGensch, T.$$b5$$uFZJ
000051048 773__ $$0PERI:(DE-600)1472258-6$$a10.1021/bi051905y$$gVol. 45, p. 5111 - 5121$$p5111 - 5121$$q45<5111 - 5121$$tBiochemistry$$v45$$x0006-2960$$y2006
000051048 8567_ $$uhttp://hdl.handle.net/2128/686$$uhttp://dx.doi.org/10.1021/bi051905y
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