Home > Publications database > Molten globule formation in apomyoglobin monitored by the fluorescent probe nile red > print

001     51048
005     20200423204325.0
024 7 _ |a pmid:16618100
|2 pmid
024 7 _ |a 10.1021/bi051905y
|2 DOI
024 7 _ |a WOS:000237049400004
|2 WOS
024 7 _ |a 2128/686
|2 Handle
037 _ _ |a PreJuSER-51048
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Polverini, E.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Molten globule formation in apomyoglobin monitored by the fluorescent probe nile red
260 _ _ |a Columbus, Ohio
|b American Chemical Society
|c 2006
300 _ _ |a 5111 - 5121
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 |a Biochemistry
|x 0006-2960
|0 798
|v 45
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The 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.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Apoproteins: chemistry
650 _ 2 |2 MeSH
|a Apoproteins: metabolism
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Computer Simulation
650 _ 2 |2 MeSH
|a Fluorescent Dyes: analysis
650 _ 2 |2 MeSH
|a Horses
650 _ 2 |2 MeSH
|a Hydrogen-Ion Concentration
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Myoglobin: chemistry
650 _ 2 |2 MeSH
|a Myoglobin: metabolism
650 _ 2 |2 MeSH
|a Oxazines: analysis
650 _ 2 |2 MeSH
|a Oxazines: chemistry
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Folding
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 7 |0 0
|2 NLM Chemicals
|a Apoproteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Fluorescent Dyes
650 _ 7 |0 0
|2 NLM Chemicals
|a Myoglobin
650 _ 7 |0 0
|2 NLM Chemicals
|a Oxazines
650 _ 7 |0 0
|2 NLM Chemicals
|a apomyoglobin
650 _ 7 |0 7385-67-3
|2 NLM Chemicals
|a nile red
650 _ 7 |a J
|2 WoSType
700 1 _ |a Cugini, G.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Annoni, F.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Abbruzzetti, S.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Viappiani, C.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Gensch, T.
|b 5
|u FZJ
|0 P:(DE-Juel1)131924
773 _ _ |a 10.1021/bi051905y
|g Vol. 45, p. 5111 - 5121
|p 5111 - 5121
|q 45<5111 - 5121
|0 PERI:(DE-600)1472258-6
|t Biochemistry
|v 45
|y 2006
|x 0006-2960
856 7 _ |u http://dx.doi.org/10.1021/bi051905y
|u http://hdl.handle.net/2128/686
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|y OpenAccess
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