This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2mag

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2mag.gif|left|200px]]<br /><applet load="2mag" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2mag.gif|left|200px]]
-
caption="2mag" />
+
 
-
'''NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES'''<br />
+
{{Structure
 +
|PDB= 2mag |SIZE=350|CAPTION= <scene name='initialview01'>2mag</scene>
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==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 <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].
+
2MAG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAG OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9090128 9090128]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/9090128 9090128]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
Line 23: Line 32:
[[Category: micelle]]
[[Category: micelle]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:22 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:46:57 2008''

Revision as of 15:46, 20 March 2008

Image:2mag.gif


PDB ID 2mag

Drag the structure with the mouse to rotate
Ligands:
Coordinates: save as pdb, mmCIF, xml



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 Thu Mar 20 17:46:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mag"
Personal tools