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1dng

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{{STRUCTURE_1dng| PDB=1dng | SCENE= }}
{{STRUCTURE_1dng| PDB=1dng | SCENE= }}
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'''NMR STRUCTURE OF A MODEL HYDROPHILIC AMPHIPATHIC HELICAL ACIDIC PEPTIDE'''
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===NMR STRUCTURE OF A MODEL HYDROPHILIC AMPHIPATHIC HELICAL ACIDIC PEPTIDE===
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==Overview==
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Sodium dodecyl sulfate (SDS) has consistently been shown to induce secondary structure, particularly alpha-helices, in polypeptides, and is commonly used to model membrane and other hydrophobic environments. However, the precise mechanism by which SDS induces these conformational changes remains unclear. To examine the role of electrostatic interactions in this mechanism, we have designed two hydrophilic, charged amphipathic alpha-helical peptides, one basic (QAPAYKKAAKKLAES) and the other acidic (QAPAYEEAAEELAKS), and their structures were studied by CD and NMR. The design of the peptides is based on the sequence of the segment of residues 56-70 of human platelet factor 4 [PF4(56-70), QAPLYKKIIKKLLES]. Both peptides were unstructured in water, and in the presence of neutral, zwitterionic, or cationic detergents. However, in SDS at neutral pH, the basic peptide folded into an alpha-helix. By contrast, the pH needed to be lowered to 1.8 before alpha-helix formation was observed for the acidic peptide. Strong, attractive electrostatic interactions, between the anionic groups of SDS and the cationic groups of the lysines, appeared to be necessary to initiate the folding of the basic peptide. NMR analysis showed that the basic peptide was fully embedded in SDS-peptide micelles, and that its three-dimensional alpha-helical structure could be superimposed on that of the native structure of PF4(56-70). These results enabled us to propose a working model of the basic peptide-SDS complex, and a mechanism for SDS-induced alpha-helical folding. This study demonstrates that, while the folding of peptides is mostly driven by hydrophobic effects, electrostatic interactions play a significant role in the formation and the stabilization of SDS-induced structure.
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{{ABSTRACT_PUBMED_10913242}}
==About this Structure==
==About this Structure==
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1DNG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DNG OCA].
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1DNG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DNG OCA].
==Reference==
==Reference==
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[[Category: De novo protein]]
[[Category: De novo protein]]
[[Category: Hydrophilic amphipathic acidic helix peptide model]]
[[Category: Hydrophilic amphipathic acidic helix peptide model]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:03:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:20:08 2008''

Revision as of 20:20, 30 June 2008

Image:1dng.png

Template:STRUCTURE 1dng

NMR STRUCTURE OF A MODEL HYDROPHILIC AMPHIPATHIC HELICAL ACIDIC PEPTIDE

Template:ABSTRACT PUBMED 10913242

About this Structure

1DNG is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Involvement of electrostatic interactions in the mechanism of peptide folding induced by sodium dodecyl sulfate binding., Montserret R, McLeish MJ, Bockmann A, Geourjon C, Penin F, Biochemistry. 2000 Jul 25;39(29):8362-73. PMID:10913242

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