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1d7n

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{{STRUCTURE_1d7n| PDB=1d7n | SCENE= }}
{{STRUCTURE_1d7n| PDB=1d7n | SCENE= }}
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'''SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS'''
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===SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11168364}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11168364 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11168364}}
==About this Structure==
==About this Structure==
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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].
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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==
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[[Category: Immune system]]
[[Category: Immune system]]
[[Category: Sodium dodecyl sulfate bound conformation]]
[[Category: Sodium dodecyl sulfate bound conformation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:32:17 2008''
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''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

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