2mag
From Proteopedia
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'''NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES''' | '''NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES''' | ||
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[[Category: Opella, S J.]] | [[Category: Opella, S J.]] | ||
[[Category: Zasloff, M.]] | [[Category: Zasloff, M.]] | ||
| - | [[Category: | + | [[Category: Amphipathic helix]] |
| - | [[Category: | + | [[Category: Antibiotic]] |
| - | [[Category: | + | [[Category: Magainin]] |
| - | [[Category: | + | [[Category: Membrane]] |
| - | [[Category: | + | [[Category: Micelle]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:31:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:31, 4 May 2008
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. 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 Sun May 4 09:31:41 2008
