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.


1d7n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1d7n.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1d7n.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1d7n| PDB=1d7n | SCENE= }}
{{STRUCTURE_1d7n| PDB=1d7n | SCENE= }}
-
'''SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS'''
+
===SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS===
-
==Overview==
+
<!--
-
Several complementary NMR approaches were used to study the interaction of mastoparan, a 14-residue peptide toxin from wasp venom, with lipid membranes. First, the 3D structure of mastoparan was determined using 1H-NMR spectroscopy in perdeuterated (SDS-d25) micelles. NOESY experiments and distance geometry calculations yielded a straight amphiphilic alpha-helix with high-order parameters, and the chemical shifts of the amide protons showed a characteristic periodicity of 3-4 residues. Secondly, solid-state 2H-NMR spectoscopy was used to describe the binding of mastoparan to lipid bilayers, composed of headgroup-deuterated dimyristoylglycerophosphocholine (DMPC-d4) and dimyristoylphosphatidylglycerol (DMPG). By correlating the deuterium quadrupole splittings of the alpha-segments and beta-segments, it was possible to differentiate the electrostatically induced structural response of the choline headgroup from dynamic effects induced by the peptide. A partial phase separation was observed, leading to a DMPG-rich phase and a DMPG-depleted phase, each containing some mastoparan. Finally, the insertion and orientation of a specifically 15N-labeled mastoparan (at position Ala10) in the bilayer environment was investigated by solid-state 15N-NMR spectroscopy, using macroscopically oriented samples. Two distinct orientational states were observed for the mastoparan helix, namely an in-plane and a trans-membrane alignment. The two populations of 90% in-plane and 10% trans-membrane helices are characterized by a mosaic spread of +/- 30 degrees and +/- 10 degrees, respectively. The biological activity of mastoparan is discussed in terms of a pore-forming model, as the peptide is known to be able to induce nonlamellar phases and facilitate a flip-flop between the monolayers.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11168364}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11168364 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11168364}}
==About this Structure==
==About this Structure==
-
1D7N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vespula_lewisii Vespula lewisii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7N OCA].
+
1D7N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vespula_lewisii Vespula lewisii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7N OCA].
==Reference==
==Reference==
Line 30: Line 34:
[[Category: Immune system]]
[[Category: Immune system]]
[[Category: Sodium dodecyl sulfate bound conformation]]
[[Category: Sodium dodecyl sulfate bound conformation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:32:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:37:58 2008''

Revision as of 19:38, 30 June 2008

Image:1d7n.png

Template:STRUCTURE 1d7n

SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS

Template:ABSTRACT PUBMED 11168364

About this Structure

1D7N is a Single protein structure of sequence from Vespula lewisii. Full experimental information is available from OCA.

Reference

Interaction of mastoparan with membranes studied by 1H-NMR spectroscopy in detergent micelles and by solid-state 2H-NMR and 15N-NMR spectroscopy in oriented lipid bilayers., Hori Y, Demura M, Iwadate M, Ulrich AS, Niidome T, Aoyagi H, Asakura T, Eur J Biochem. 2001 Jan;268(2):302-9. PMID:11168364

Page seeded by OCA on Mon Jun 30 22:37:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1d7n"
Personal tools