1d7n
From Proteopedia
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'''SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS''' | '''SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS''' | ||
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[[Category: Iwadate, M.]] | [[Category: Iwadate, M.]] | ||
[[Category: Niidome, T.]] | [[Category: Niidome, T.]] | ||
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| - | [[Category: | + | [[Category: Sodium dodecyl sulfate bound conformation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:32:17 2008'' | |
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Revision as of 10:32, 2 May 2008
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.
About this Structure
1D7N is a Single protein structure of sequence from Vespula lewisii. Full crystallographic 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 Fri May 2 13:32:17 2008
