1l4x: Difference between revisions
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'''octameric de novo designed peptide''' | '''octameric de novo designed peptide''' | ||
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==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4X OCA]. | |||
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/12064934 12064934] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12064934 12064934] | ||
[[Category: Aebi, U.]] | [[Category: Aebi, U.]] | ||
[[Category: Burkhard, P.]] | [[Category: Burkhard, P.]] | ||
[[Category: Lustig, A.]] | [[Category: Lustig, A.]] | ||
[[Category: Meier, M.]] | [[Category: Meier, M.]] | ||
[[Category: | [[Category: Coiled coil]] | ||
[[Category: | [[Category: Ionic interaction]] | ||
[[Category: | [[Category: Protein de novo design]] | ||
[[Category: | [[Category: Protein folding]] | ||
[[Category: | [[Category: Protein oligomerization]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:32:36 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 20:32, 2 May 2008
octameric de novo designed peptide
Overview
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.
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 Fri May 2 23:32:36 2008
