[NMR paper] Magic angle spinning (31)P NMR spectroscopy reveals two essentially identical ionization states for the cardiolipin phosphates in phospholipid liposomes.
Magic angle spinning (31)P NMR spectroscopy reveals two essentially identical ionization states for the cardiolipin phosphates in phospholipid liposomes.
Related ArticlesMagic angle spinning (31)P NMR spectroscopy reveals two essentially identical ionization states for the cardiolipin phosphates in phospholipid liposomes.
Abstract
Specific membrane lipid composition is crucial for optimized structural and functional organization of biological membranes. Cardiolipin is a unique phospholipid and important component of the inner mitochondrial membrane. It is involved in energy metabolism, inner mitochondrial membrane transport, regulation of multiple metabolic reactions and apoptotic cell death. The physico-chemical properties of cardiolipin have been studied extensively but despite all these efforts there is still lingering controversy regarding the ionization of the two phosphate groups of cardiolipin. Results obtained in the 1990s and early 2000s suggested that cardiolipin has two disparate pKa values where one of the protons was proposed to be stabilized by an intramolecular hydrogen bond. This has led to extensive speculations on the roles of these two putative ionization states of cardiolipin in mitochondria. More recently the notion of two pKa values has been challenged and rejected by several groups. These studies relied on external measurements of proton adsorption or electrophoretic mobility of membranes but did not take into account the low pH phase behavior and chemical stability of cardiolipin. Here we used (31)P NMR to show that in the physiologically relevant membrane phospholipid environment, cardiolipin carries two negative charges at physiological pH. We additionally demonstrate the pH dependent phase behavior and chemical stability of cardiolipin containing membranes.
PMID: 27984017 [PubMed - as supplied by publisher]
[NMR paper] Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.
Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.
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Methods Mol Biol. 2016;1345:173-83
Authors: Tuttle MD, Courtney JM, Barclay AM, Rienstra CM
Abstract
Solid-state NMR spectroscopy (SSNMR) is an established and invaluable tool for the study of amyloid fibril structure with atomic-level detail. Optimization of the homogeneity and concentration of fibrils enhances the resolution and sensitivity...
[NMR paper] Quadruple-Resonance Magic-Angle Spinning NMR Spectroscopy of Deuterated Solid Proteins.
Quadruple-Resonance Magic-Angle Spinning NMR Spectroscopy of Deuterated Solid Proteins.
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Angew Chem Int Ed Engl. 2014 Jan 29;
Authors: Akbey U, Nieuwkoop AJ, Wegner S, Voreck A, Kunert B, Bandara P, Engelke F, Nielsen NC, Oschkinat H
Abstract
(1) H-detected magic-angle spinning NMR experiments facilitate structural biology of solid proteins, which requires using deuterated proteins. However, often amide protons cannot be back-exchanged...
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[NMR paper] Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
J Am Chem Soc. 2013 Oct 28;
Authors: Han Y, Hou G, Suiter CL, Ahn J, Byeon IJ, Lipton AS, Burton SD, Hung I, Gor'kov PL, Gan Z, Brey WW, Rice D, Gronenborn AM, Polenova TE
Abstract
A key stage in HIV-1 maturation towards...
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[NMR paper] Full-length Vpu and human CD4(372-433) in phospholipid bilayers as seen by magic angle spinning NMR.
Full-length Vpu and human CD4(372-433) in phospholipid bilayers as seen by magic angle spinning NMR.
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Biol Chem. 2013 Jul 17;
Authors: Do HQ, Wittlich M, Glück JM, Möckel L, Willbold D, Koenig BW, Heise H
Abstract
Abstract HIV-1 Vpu and CD4(372-433), a peptide comprising the transmembrane and cytoplasmic domain of human CD4, were recombinantly expressed in Escherichia coli, uniformly labeled with 13C und 15N isotopes,...
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Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Biochim Biophys Acta. 2011 Aug 3;
Authors: Gustavsson M, Traaseth NJ, Veglia G
In this paper, we analyzed the ground and excited states of phospholamban (PLN), a membrane protein that regulates sarcoplasmic reticulum calcium ATPase (SERCA), in different membrane mimetic environments....
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[NMR paper] Magic angle spinning solid-state NMR spectroscopy for structural studies of protein i
Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
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J Am Chem Soc. 2004 Dec 22;126(50):16608-20
Authors: Marulanda D, Tasayco ML, McDermott A, Cataldi M, Arriaran V,...
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[NMR paper] Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle sp
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Biochemistry. 1992 Oct 20;31(41):10129-38
Authors: Spooner PJ, Watts A
The influence of cytochrome c binding to cardiolipin bilayers on the motional characteristics of each component has been analyzed by magic-angle spinning (MAS) NMR. Observations were made by NMR of natural abundance 31P, 13C, and 1H nuclei in the lipid as...
Magic angle spinning (31)P NMR spectroscopy reveals two essentially identical ionization states for the cardiolipin phosphates in phospholipid liposomes.
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