Related ArticlesCytochrome 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 spectroscopy of the protein heme group and 31P NMR of the phospholipid headgroups. The gel-to-fluid-phase transition of dimyristoylphosphatidylglycerol induces shifts in the conformational and coordination equilibria of the bound cytochrome c, as recorded by the resonance Raman spectra in the fingerprint and marker band regions. Conformational and coordination shifts of the bound cytochrome are also induced on admixture of dioleoylglycerol or dioleoylphosphatidylcholine with dioleoylphosphatidylglycerol. In the case of dioleoylglycerol, significant changes take place even at levels as low as 5 mol %. Binding of cytochrome c induces or increases the content of near isotropically diffusing lipid registered by the 31P NMR spectra of the different lipids studied. Admixture of dioleoylglycerol also increases the bilayer curvature of dioleoylphosphatidylglycerol, inducing an inverted hexagonal phase at 50 mol % concentration; the tendency to spontaneous curvature in the lipid appears to relax the conformational change detected in the protein.
Skeletal muscle lipid metabolism studied by advanced magnetic resonance spectroscopy
Skeletal muscle lipid metabolism studied by advanced magnetic resonance spectroscopy
Publication year: 2012
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, Available online 23 February 2012</br>
Arunima*Pola, Suresh Anand*Sadananthan, Jadegoud*Yaligar, Vijayasarathi*Nagarajan, Weiping*Han, ...</br>
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[NMR paper] Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy wit
Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents.
Related Articles Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents.
Chembiochem. 2004 Apr 2;5(4):467-73
Authors: Hilty C, Wider G, Fernández C, Wüthrich K
For solution NMR studies of the structure and function of membrane proteins, these macromolecules have to be reconstituted and solubilized in detergent micelles. Detailed characterization of the mixed...
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11-24-2010 09:51 PM
[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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11-24-2010 08:58 PM
[NMR paper] Lipid specificity in the interaction of cytochrome c with anionic phospholipid bilaye
Lipid specificity in the interaction of cytochrome c with anionic phospholipid bilayers revealed by solid-state 31P NMR.
Related Articles Lipid specificity in the interaction of cytochrome c with anionic phospholipid bilayers revealed by solid-state 31P NMR.
Biochemistry. 1994 Mar 8;33(9):2451-8
Authors: Pinheiro TJ, Watts A
Phosphorus-31 NMR has been used to investigate the interaction of cytochrome c with bilayers of the anionic lipids dioleoylphosphatidylglycerol (DOPG), dioleoylphosphatidylserine (DOPS), and diacylphosphatidylinositol...
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[NMR paper] Interactions of phospholipids with the mitochondrial cytochrome-c reductase studied b
Interactions of phospholipids with the mitochondrial cytochrome-c reductase studied by spin-label ESR and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Interactions 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...
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08-21-2010 11:45 PM
[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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08-21-2010 11:12 PM
[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...