Related ArticlesInvestigation of oxidation state-dependent conformational changes in Desulfovibrio vulgaris Hildenborough cytochrome c553 by two-dimensional H-NMR spectra.
FEBS Lett. 1996 Jul 1;389(2):203-9
Authors: Blanchard L, Blackledge MJ, Marion D, Guerlesquin F
Two-dimensional nuclear magnetic resonance spectroscopy (2D-NMR) was used to assign the proton resonances of ferricytochrome C553 from Desulfovibrio vulgaris Hildenborough. The spin systems of 76 out of 79 amino acids were identified by J-correlation spectroscopy (COSY and HOHAHA) in H20 and D20 and correlated by nuclear Overhauser effect spectroscopy (NOESY). The proton chemical shifts are compared in both oxidized and reduced states of the protein at 23 degrees C and pH 5.9. Chemical shift variations between reduced and oxidized states are due to the paramagnetic contribution. Medium and long-range nOe demonstrate the lack of major changes between the two redox states. NMR data provide evidence that in this low oxidoreduction potential cytochrome, the oxidized state is more rigid than the reduced state.
Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy
Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy
Abstract Cytochrome c (Cc) is a soluble electron carrier protein, transferring reducing equivalents between Cc reductase and Cc oxidase in eukaryotes. In this work, we assessed the structural differences between reduced and oxidized Cc in solution by paramagnetic NMR spectroscopy. First, we have obtained nearly-complete backbone NMR resonance assignments for iso-1-yeast Cc and horse Cc in both oxidation states. These were further used to derive pseudocontact shifts (PCSs) arising...
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[NMR paper] NMR investigation of the alkaline-like conformational transition of horse heart cytoc
NMR investigation of the alkaline-like conformational transition of horse heart cytochrome c in the presence of exogenous thiazole.
Related Articles NMR investigation of the alkaline-like conformational transition of horse heart cytochrome c in the presence of exogenous thiazole.
Biophys Chem. 2003 Jun 1;104(2):459-68
Authors: Yao Y, Tang W
The conformational transition of horse heart cyt c in the presence of exogenous thiazole is investigated by NMR spectroscopy. Surprisingly, besides the native form and the ligand-bound form, another species...
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[NMR paper] Metal-dependent conformational changes in a recombinant vWF-A domain from human facto
Metal-dependent conformational changes in a recombinant vWF-A domain from human factor B: a solution study by circular dichroism, fourier transform infrared and (1)H NMR spectroscopy.
Related Articles Metal-dependent conformational changes in a recombinant vWF-A domain from human factor B: a solution study by circular dichroism, fourier transform infrared and (1)H NMR spectroscopy.
J Mol Biol. 2000 Apr 21;298(1):135-47
Authors: Hinshelwood J, Perkins SJ
Factor B is a key component of the alternative pathway of complement and is cleaved by...
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[NMR paper] An NMR investigation of the conformational effect of nitroxide spin labels on Ala-ric
An NMR investigation of the conformational effect of nitroxide spin labels on Ala-rich helical peptides.
Related Articles An NMR investigation of the conformational effect of nitroxide spin labels on Ala-rich helical peptides.
J Magn Reson. 1998 Apr;131(2):248-53
Authors: Bolin KA, Hanson P, Wright SJ, Millhauser GL
Nitroxide spin labels, in conjunction with electron spin resonance (ESR) experiments, are extensively employed to probe the structure and dynamics of biomolecules. One of the most ubiquitous spin labeling reagents is the...
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[NMR paper] Evidence for oxidation-state-dependent conformational changes in human ferredoxin fro
Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy.
Related Articles Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy.
Biochemistry. 1998 Mar 17;37(11):3965-73
Authors: Xia B, Volkman BF, Markley JL
Human ferredoxin belongs to the vertebrate ferredoxin family which includes bovine adrenodoxin. It is a small (13.8 kDa) acidic protein with a cluster. It functions as an electron...
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[NMR paper] Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution
Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution by heteronuclear-edited proton-observed NMR methods.
Related Articles Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution by heteronuclear-edited proton-observed NMR methods.
Biochemistry. 1993 Jul 6;32(26):6763-72
Authors: Hu JS, Redfield AG
Heteronuclear-edited proton-detected NMR methods are used to study the nucleotide-dependent conformational change between GDP- and GTP gamma S-bound forms of human N-ras p21. Amide...
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[NMR paper] 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conf
1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c.
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 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c.
Eur J Biochem. 1993 Feb 1;211(3):555-62
Authors: Turner DL, Williams RJ
The redox-state dependent changes in chemical shift, which have...
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[NMR paper] Investigation of the Ca2(+)-dependent interaction of trifluoperazine with S100a: a 19
Investigation of the Ca2(+)-dependent interaction of trifluoperazine with S100a: a 19F NMR and circular dichroism study.
Related Articles Investigation of the Ca2(+)-dependent interaction of trifluoperazine with S100a: a 19F NMR and circular dichroism study.
J Protein Chem. 1990 Apr;9(2):169-75
Authors: Pingerelli PL, Mizukami H, Wagner AS, Bartnicki DE, Oliver JP
S100a is a heterodimeric, acidic calcium-binding protein that interacts with calmodulin antagonists in a Ca2(+)-dependent manner. In order to study the behavior of the hydrophobic...