Related ArticlesInteractions of phospholipids with the mitochondrial cytochrome-c reductase studied by spin-label ESR and NMR spectroscopy.
Eur J Biochem. 1992 Oct 1;209(1):423-30
Authors: Hayer-Hartl M, Schägger H, von Jagow G, Beyer K
Protein/phospholipid interactions in the solubilized mitochondrial ubihydroquinone:cytochrome-c oxidoreductase (bc1 complex) were studied by spin-label electron-spin resonance and by 31P-NMR spectroscopy. Spin-labelled phospholipids were employed to probe the relative binding affinities of a number of phospholipids with regard to the significance of phospholipids for the activity and stability of this multisubunit complex. The protein was titrated with spin-labelled cardiolipin (1,3-bisphosphatidyl-sn-glycerol) and with the spin-labelled analogues of PtdCho and PtdEtn, both of which have been shown recently to elicit a substantial increase in electron-transport activity [Schägger, H., Hagen, T., Roth, B., Brandt, U., Link, T. A. & von Jagow, G. (1990) Eur. J. Biochem. 190, 123-130]. A simplified distribution model showed that neutral phospholipids have much lower protein affinity than cardiolipin. In contrast to the transient weak lipid binding detected by spin-label electron-spin resonance, 31P NMR revealed a tightly bound cardiolipin portion, even after careful delipidation of the complex. Considerable line narrowing was observed after phospholipase A2 digestion of the bound cardiolipin, whereas addition of SDS resulted in complete release. Relative proportions and line widths of mobile and immobilized lipids were obtained by deconvoluting the partially overlapping signals. The current results are discussed with reference to similar findings with other mitochondrial membrane proteins. It is assumed that activation by neutral phospholipids reflects a generalized effect on the protein conformation. Cardiolipin binding is believed to be important for the structural integrity of the mitochondrial protein complexes.
Structure of the lipodepsipeptide syringomycin E in phospholipids and sodium dodecylsulphate micelle studied by circular dichroism, NMR spectroscopy and molecular dynamics.
Structure of the lipodepsipeptide syringomycin E in phospholipids and sodium dodecylsulphate micelle studied by circular dichroism, NMR spectroscopy and molecular dynamics.
Structure of the lipodepsipeptide syringomycin E in phospholipids and sodium dodecylsulphate micelle studied by circular dichroism, NMR spectroscopy and molecular dynamics.
Biochim Biophys Acta. 2011 Sep;1808(9):2102-10
Authors: Anselmi M, Eliseo T, Zanetti-Polzi L, Fullone MR, Fogliano V, Di Nola A, Paci M, Grgurina I
Abstract
Syringomycin E (SRE) is a member of a...
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[NMR paper] Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C
Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin.
Related Articles Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin.
Biochemistry. 2003 Jun 17;42(23):7068-76
Authors: Worrall JA, Reinle W, Bernhardt R, Ubbink M
The interaction between yeast iso-1-cytochrome c (C102T) and two forms of bovine adrenodoxin, the wild type and a truncated form comprising residues 4-108, has been investigated using a combination of one- and two-dimensional...
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[NMR paper] The interactions of cyanobacterial cytochrome c6 and cytochrome f, characterized by N
The interactions of cyanobacterial cytochrome c6 and cytochrome f, characterized by NMR.
Related Articles The interactions of cyanobacterial cytochrome c6 and cytochrome f, characterized by NMR.
J Biol Chem. 2002 Dec 13;277(50):48685-9
Authors: Crowley PB, Díaz-Quintana A, Molina-Heredia FP, Nieto P, Sutter M, Haehnel W, De La Rosa MA, Ubbink M
During oxygenic photosynthesis, cytochrome c(6) shuttles electrons between the membrane-bound complexes cytochrome bf and photosystem I. Complex formation between Phormidium laminosum cytochrome f and...
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[NMR paper] Cytochrome c-lipid interactions studied by resonance Raman and 31P NMR spectroscopy.
Cytochrome c-lipid interactions studied by resonance Raman and 31P NMR spectroscopy. Correlation between the conformational changes of the protein and the lipid bilayer.
Related Articles Cytochrome c-lipid interactions studied by resonance Raman and 31P NMR spectroscopy. Correlation between the conformational changes of the protein and the lipid bilayer.
Biochemistry. 1991 Sep 17;30(37):9084-9
Authors: Heimburg T, Hildebrandt P, Marsh D
The interaction of cytochrome c with negatively charged lipids has been studied by resonance Raman...
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[NMR paper] Cytochrome c-lipid interactions studied by resonance Raman and 31P NMR spectroscopy.
Cytochrome c-lipid interactions studied by resonance Raman and 31P NMR spectroscopy. Correlation between the conformational changes of the protein and the lipid bilayer.
Related Articles Cytochrome c-lipid interactions studied by resonance Raman and 31P NMR spectroscopy. Correlation between the conformational changes of the protein and the lipid bilayer.
Biochemistry. 1991 Sep 17;30(37):9084-9
Authors: Heimburg T, Hildebrandt P, Marsh D
The interaction of cytochrome c with negatively charged lipids has been studied by resonance Raman...
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[NMR paper] NMR studies of interactions of ligands with dihydrofolate reductase.
NMR studies of interactions of ligands with dihydrofolate reductase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of interactions of ligands with dihydrofolate reductase.
Biochem Pharmacol. 1990 Jul 1;40(1):141-52
Authors: Feeney J
NMR spectroscopy is a useful technique for studying interactions, conformations and dynamic processes within ligand-protein complexes. Several examples of the application of the method to studies of complexes of anti-folate...
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[NMR paper] Salt-dependent structure change and ion binding in cytochrome c studied by two-dimens
Salt-dependent structure change and ion binding in cytochrome c studied by two-dimensional proton NMR.
Related Articles Salt-dependent structure change and ion binding in cytochrome c studied by two-dimensional proton NMR.
Biochemistry. 1990 Apr 10;29(14):3505-9
Authors: Feng Y, Englander SW
To search for salt-dependent structure changes that might help to explain physicochemical differences observed in previous solution studies, two-dimensional proton NMR spectra of reduced and oxidized cytochrome c were recorded at relatively high and low...
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[NMR paper] NMR characterization of surface interactions in the cytochrome b5-cytochrome c comple
NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex.
Related Articles NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex.
Science. 1990 Feb 16;247(4944):831-3
Authors: Burch AM, Rigby SE, Funk WD, MacGillivray RT, Mauk MR, Mauk AG, Moore GR
The complex formed in solution by native and chemically modified cytochrome c with cytochrome b5 has been studied by 1H and 13C nuclear magnetic resonance spectroscopy (NMR). Contrary to predictions of recent theoretical analysis, 1H NMR...
Interactions of phospholipids with the mitochondrial cytochrome-c reductase studied b
Linear Mode
