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1l4x

From Proteopedia

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[[Image:1l4x.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1l4x| PDB=1l4x | SCENE= }}
{{STRUCTURE_1l4x| PDB=1l4x | SCENE= }}
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'''octameric de novo designed peptide'''
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===octameric de novo designed peptide===
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==Overview==
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Alpha-helical coiled coils represent a common protein oligomerization motif that are mainly stabilized by hydrophobic interactions occurring along their coiled-coil interface, the so-called hydrophobic seam. We have recently de novo designed and optimized a series of two-heptad repeat long coiled-coil peptides which are further stabilized by a complex network of inter- and intrahelical salt bridges. Here we have extended the de novo design of such two heptad-repeat long peptides by removing the central and most important g-e' Arg to Glu (g-e'RE) ionic interhelical interaction and replacing these residues by alanine residues. The effect of the missing interhelical ionic interaction on coiled-coil formation and stability has been analyzed by CD spectroscopy, analytical ultracentrifugation, and X-ray crystallography. We show that the peptide, while being highly alpha-helical, is no longer able to form a parallel coiled-coil structure but rather assumes an octameric globular helical assembly devoid of any coiled-coil interactions.
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The line below this paragraph, {{ABSTRACT_PUBMED_12064934}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12064934 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12064934}}
==About this Structure==
==About this Structure==
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[[Category: Protein folding]]
[[Category: Protein folding]]
[[Category: Protein oligomerization]]
[[Category: Protein oligomerization]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:32:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:42:37 2008''

Revision as of 08:42, 2 July 2008

Image:1l4x.png

Template:STRUCTURE 1l4x

octameric de novo designed peptide

Template:ABSTRACT PUBMED 12064934

About this Structure

Full crystallographic information is available from OCA.

Reference

Removing an interhelical salt bridge abolishes coiled-coil formation in a de novo designed peptide., Meier M, Lustig A, Aebi U, Burkhard P, J Struct Biol. 2002 Jan-Feb;137(1-2):65-72. PMID:12064934

Page seeded by OCA on Wed Jul 2 11:42:37 2008

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