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2mag
From Proteopedia
(New page: 200px<br /><applet load="2mag" size="450" color="white" frame="true" align="right" spinBox="true" caption="2mag" /> '''NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES,...) |
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| - | [[Image:2mag.gif|left|200px]]<br /><applet load="2mag" size=" | + | [[Image:2mag.gif|left|200px]]<br /><applet load="2mag" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES'''<br /> | '''NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Magainin2 is a 23-residue antibiotic peptide that disrupts the ionic | + | Magainin2 is a 23-residue antibiotic peptide that disrupts the ionic gradient across certain cell membranes. Two-dimensional 1H NMR spectroscopy was used to investigate the structure of the peptide in three of the membrane environments most commonly employed in biophysical studies. Sequence-specific resonance assignments were determined for the peptide in perdeuterated dodecylphosphocholine (DPC) and sodium dodecylsulfate micelles and confirmed for the peptide in 2,2,2-trifluoroethanol solution. The secondary structure is shown to be helical in all of the solvent systems. The NMR data were used as a set of restraints for a simulated annealing protocol that generated a family of three-dimensional structures of the peptide in DPC micelles, which superimposed best between residues 4 and 20. For these residues, the mean pairwise rms difference for the backbone atoms is 0.47 +/- 0.10 A from the average structure. The calculated peptide structures appear to be curved, with the bend centered at residues Phe12 and Gly13. |
==About this Structure== | ==About this Structure== | ||
| - | 2MAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2MAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
| - | [[Category: Gesell, J | + | [[Category: Gesell, J J.]] |
| - | [[Category: Opella, S | + | [[Category: Opella, S J.]] |
[[Category: Zasloff, M.]] | [[Category: Zasloff, M.]] | ||
[[Category: NH2]] | [[Category: NH2]] | ||
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[[Category: micelle]] | [[Category: micelle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:22 2008'' |
Revision as of 16:07, 21 February 2008
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NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES
Overview
Magainin2 is a 23-residue antibiotic peptide that disrupts the ionic gradient across certain cell membranes. Two-dimensional 1H NMR spectroscopy was used to investigate the structure of the peptide in three of the membrane environments most commonly employed in biophysical studies. Sequence-specific resonance assignments were determined for the peptide in perdeuterated dodecylphosphocholine (DPC) and sodium dodecylsulfate micelles and confirmed for the peptide in 2,2,2-trifluoroethanol solution. The secondary structure is shown to be helical in all of the solvent systems. The NMR data were used as a set of restraints for a simulated annealing protocol that generated a family of three-dimensional structures of the peptide in DPC micelles, which superimposed best between residues 4 and 20. For these residues, the mean pairwise rms difference for the backbone atoms is 0.47 +/- 0.10 A from the average structure. The calculated peptide structures appear to be curved, with the bend centered at residues Phe12 and Gly13.
About this Structure
2MAG is a Single protein structure of sequence from Xenopus laevis with as ligand. Full crystallographic information is available from OCA.
Reference
Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution., Gesell J, Zasloff M, Opella SJ, J Biomol NMR. 1997 Feb;9(2):127-35. PMID:9090128
Page seeded by OCA on Thu Feb 21 18:07:22 2008
Categories: Single protein | Xenopus laevis | Gesell, J J. | Opella, S J. | Zasloff, M. | NH2 | Amphipathic helix | Antibiotic | Magainin | Membrane | Micelle
