Related ArticlesDynamic pictures of membrane proteins in two-dimensional crystal, lipid bilayer and detergent as revealed by site-directed solid-state 13C NMR.
Chem Phys Lipids. 2004 Nov;132(1):101-12
Authors: Saitô H
We have compared site-directed 13C solid-state NMR spectra of [3-13C]Ala- and/or [1-13C]Val-labeled membrane proteins, including bacteriorhodopsin (bR), pharaonis phoborhodopin (ppR), its cognate transducer (pHtrII) and Escherichia coli diacylglycerol kinase (DGK), in two-dimensional (2D) crystal, lipid bilayers, and detergent. Restricted fluctuation motions of these membrane proteins due to oligomerization of bR by specific protein-protein interactions in the 2D crystalline lattice or protein complex between ppR and pHtrII provide the most favorable environment to yield well-resolved, fully visible 13C NMR signals for [3-13C]Ala-labeled proteins. In contrast, several signals from such membrane proteins were broadened or lost owing to interference of inherent fluctuation frequencies (10(4)-10(5)Hz) with frequency of either proton decoupling or magic angle spinning, if their 13C NMR spectra were recorded as a monomer in lipid bilayers at ambient temperature. The presence of such protein dynamics is essential for the respective proteins to achieve their own biological functions. Finally, spectral broadening found for bR and DGK in detergents were discussed.
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...
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Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Biophys J. 2010 Nov 17;99(10):3282-9
Authors: Toraya S, Javkhlantugs N, Mishima D, Nishimura K, Ueda K, Naito A
Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to...
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03-03-2011 12:34 PM
The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.
The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.
The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.
Structure. 2010 Oct 13;18(10):1280-8
Authors: Kalli AC, Wegener KL, Goult BT, Anthis NJ, Campbell ID, Sansom MS
Integrins are cell surface receptors crucial for cell migration and adhesion. They are activated by interactions of the talin head domain with the membrane surface and the integrin ? cytoplasmic tail. Here, we use coarse-grained molecular dynamic...
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03-03-2011 12:34 PM
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
J Struct Funct Genomics. 2010 Dec 14;
Authors: Mani R, Vorobiev S, Swapna GV, Neely H, Janjua H, Ciccosanti C, Xiao R, Acton TB, Everett JK, Hunt J, Montelione GT
The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the Northeast Structural...
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12-15-2010 12:03 PM
A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.
A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.
Related Articles A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.
Structure. 2010 Dec 8;18(12):1559-1569
Authors: Call ME, Chou JJ
One of the most fundamental problems in cell biology concerns how cells communicate with their surroundings through surface receptors. The last few decades have seen major advances in understanding the mechanisms of receptor-ligand...
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12-08-2010 06:21 PM
[NMR paper] Investigating structural changes in the lipid bilayer upon insertion of the transmemb
Investigating structural changes in the lipid bilayer upon insertion of the transmembrane domain of the membrane-bound protein phospholamban utilizing 31P and 2H solid-state NMR spectroscopy.
Related Articles Investigating structural changes in the lipid bilayer upon insertion of the transmembrane domain of the membrane-bound protein phospholamban utilizing 31P and 2H solid-state NMR spectroscopy.
Biophys J. 2004 Mar;86(3):1564-73
Authors: Dave PC, Tiburu EK, Damodaran K, Lorigan GA
Phospholamban (PLB) is a 52-amino acid integral membrane...
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11-24-2010 09:25 PM
[NMR paper] Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimension
Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimensional array formation as revealed by site-directed solid-state 13C NMR studies on Ala- and Val-labeled bacteriorhodopsin.
Related Articles Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimensional array formation as revealed by site-directed solid-state 13C NMR studies on Ala- and Val-labeled bacteriorhodopsin.
Biochim Biophys Acta. 2003 Oct 13;1616(2):127-36
Authors: Saitô H, Yamamoto K, Tuzi S, Yamaguchi S
We have recorded...
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11-24-2010 09:16 PM
[NMR paper] Structure of gramicidin a in a lipid bilayer environment determined using molecular d
Structure of gramicidin a in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data.
Related Articles Structure of gramicidin a in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data.
J Am Chem Soc. 2003 Aug 13;125(32):9868-77
Authors: Allen TW, Andersen OS, Roux B
Two different high-resolution structures recently have been proposed for the membrane-spanning gramicidin A channel: one based on solid-state NMR experiments in oriented phospholipid...
Dynamic pictures of membrane proteins in two-dimensional crystal, lipid bilayer and d
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