Related ArticlesInteraction of a type II myosin with biological membranes studied by 2H solid state NMR.
Biochemistry. 1998 Apr 21;37(16):5582-8
Authors: Arêas JA, Gröbner G, Glaubitz C, Watts A
Deuterium nuclear magnetic resonance spectroscopy (2H NMR) has been employed to investigate the interaction of lung type II myosin protein with neutral bilayers containing dimyristoylphosphatidylcholine (DMPC) as the only constituent and mixed bilayers containing the negatively charged lipid dimyristoylphosphatidylglycerol (DMPG). DMPC was deuterated at its headgroup by substituting the four protons at the alpha- and beta-positions (DMPC-d4) and the nine protons at the gamma-position (DMPC-d9). DMPG was perdeuterated at its headgroup (DMPG-d5). No changes were observed in the quadrupole splittings or spin-lattice relaxation times for the deuterated DMPC headgroup segments when increasing amounts of myosin were added to liposomes, made exclusively of DMPC-d9 or of DMPC-d4. However, upon the insertion of the negatively charged lipid DMPG at 1:1 molar ratio into the DMPC bilayers, myosin was found to interact electrostatically with the liposomes, thereby affecting significantly both the quadrupole splittings and spin-lattice relaxation rates of the alpha-, beta-, and gamma-deuterons in labeled DMPC. Monitoring DMPG-d5 in mixed DMPC/DMPG bilayers revealed a direct electrostatic interaction of DMPG with the protein, where positively charged lysine residues located at the tail domain of myosin provide the necessary sites for the interaction to occur. When ATP and Mg2+ were complexed to the head domain of myosin, a reduced interaction with the negatively charged bilayers was observed. The results clearly indicate that a type II myosin can interact with membranes without the need for a specific hydrophobic domain or an anchor in the protein molecule, provided that negatively charged lipids are present in the bilayer.
The interaction of cannabinoid receptor agonists, CP55940 and WIN55212-2 with membranes using solid state 2H NMR.
The interaction of cannabinoid receptor agonists, CP55940 and WIN55212-2 with membranes using solid state 2H NMR.
The interaction of cannabinoid receptor agonists, CP55940 and WIN55212-2 with membranes using solid state 2H NMR.
Biochim Biophys Acta. 2011 Sep;1808(9):2095-101
Authors: Tian X, Pavlopoulos S, Yang DP, Makriyannis A
Abstract
Two key commonly used cannabinergic agonists, CP55940 and WIN55212-2, are investigated for their effects on the lipid membrane bilayer using (2)H solid state NMR, and the results are compared with our...
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09-13-2011 08:27 PM
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
J Am Chem Soc. 2011 Jul 21;
Authors: Fu R, Wang X, Li C, Santiago-Miranda AN, Pielak GJ, Tian F
The feasibility of using solid state MAS NMR for in situ structural characterization of the LR11 (sorLA) transmembrane domain in native Escherichia coli (E. coli) membranes is presented. LR11 interacts with...
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07-23-2011 08:54 AM
Solid-State (19)F-NMR of Peptides in Native Membranes.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Top Curr Chem. 2011 May 20;
Authors: Koch K, Afonin S, Ieronimo M, Berditsch M, Ulrich AS
To understand how membrane-active peptides (MAPs) function in vivo, it is essential to obtain structural information about them in their membrane-bound state. Most biophysical approaches rely on the use of bilayers prepared from synthetic phospholipids, i.e. artificial model membranes. A particularly successful structural method is solid-state NMR,...
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05-21-2011 07:51 PM
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Eur Biophys J. 2011 Jan 28;
Authors: Grasnick D, Sternberg U, Strandberg E, Wadhwani P, Ulrich AS
To better understand peptide-induced membrane fusion at a molecular level, we set out to determine the structure of the fusogenic peptide FP23 from the HIV-1 protein gp41 when bound to a lipid bilayer. An established solid-state...
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01-29-2011 12:35 PM
[NMR paper] Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes st
Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes studied by solid state NMR.
Related Articles Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes studied by solid state NMR.
Chem Phys Lipids. 2004 Nov;132(1):65-77
Authors: Grage SL, Afonin S, Grüne M, Ulrich AS
The interaction of the fusogenic polypeptide segment "B18" from the fertilization protein binding with lipid membranes was investigated by solid state 2H and 31P NMR, and by differential scanning calorimetry. B18 is known...
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11-24-2010 10:03 PM
[NMR paper] Exploring the calcium-binding site in photosystem II membranes by solid-state (113)Cd
Exploring the calcium-binding site in photosystem II membranes by solid-state (113)Cd NMR.
Related Articles Exploring the calcium-binding site in photosystem II membranes by solid-state (113)Cd NMR.
Biochemistry. 2000 Jun 13;39(23):6751-5
Authors: Matysik J, Alia A, Nachtegaal G, van Gorkom HJ, Hoff AJ, de Groot HJ
Calcium (Ca(2+)) is an essential cofactor for photosynthetic oxygen evolution. Although the involvement of Ca(2+) at the oxidizing side of photosystem II of plants has been known for a long time, its ligand interactions and mode of...
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11-18-2010 09:15 PM
[NMR paper] Solid-state NMR studies of magnetically aligned phospholipid membranes: taming lantha
Solid-state NMR studies of magnetically aligned phospholipid membranes: taming lanthanides for membrane protein studies.
Related Articles Solid-state NMR studies of magnetically aligned phospholipid membranes: taming lanthanides for membrane protein studies.
Biochem Cell Biol. 1998;76(2-3):443-51
Authors: Prosser RS, Volkov VB, Shiyanovskaya IV
The addition of lanthanides (Tm3+, Yb3+, Er3+, or Eu3+) to a solution of long-chain phospholipids such as dimyristoylphosphatidylcholine (DMPC) and short-chain phospholipids such as...
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Post-Doc position in biological solid-State NMR
Post-Doc position in biological solid-State NMR
The biological solid-state NMR group of Anja Böckmann at the IBCP in Lyon (www.ibcp.fr) has an opening for a post-doc.
The project is part of the Bio-NMR European joint research activity on protein structure determination by solid-state NMR, and is a collaboration which is pursued with the groups of Beat H. Meier (ETH Zurich) and Peter Güntert (University of Frankfurt). It involves production and purification of model proteins, starte-of-the-art spectroscopy, spectral analysis and structure determination. It is the aim of the project to...
Interaction of a type II myosin with biological membranes studied by 2H solid state N
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