1u9f
From Proteopedia
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[[Image:1u9f.jpg|left|200px]] | [[Image:1u9f.jpg|left|200px]] | ||
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'''Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(15)L(16)''' | '''Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(15)L(16)''' | ||
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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=1U9F OCA]. | |
==Reference== | ==Reference== | ||
Heterocyclic peptide backbone modifications in an alpha-helical coiled coil., Horne WS, Yadav MK, Stout CD, Ghadiri MR, J Am Chem Soc. 2004 Dec 1;126(47):15366-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15563148 15563148] | Heterocyclic peptide backbone modifications in an alpha-helical coiled coil., Horne WS, Yadav MK, Stout CD, Ghadiri MR, J Am Chem Soc. 2004 Dec 1;126(47):15366-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15563148 15563148] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Ghadiri, M R.]] | [[Category: Ghadiri, M R.]] | ||
[[Category: Horne, W S.]] | [[Category: Horne, W S.]] | ||
[[Category: Stout, C D.]] | [[Category: Stout, C D.]] | ||
[[Category: Yadav, M K.]] | [[Category: Yadav, M K.]] | ||
| - | [[Category: | + | [[Category: Heterocycic backbone modification]] |
| - | [[Category: | + | [[Category: Tetrameric alpha-helical coiled coil]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:55:56 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:55, 3 May 2008
Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(15)L(16)
Overview
In this paper, we present 1,2,3-triazole epsilon2-amino acids incorporated as a dipeptide surrogate at three positions in the sequence of a known alpha-helical coiled coil. Biophysical characterization indicates that the modified peptides retain much of the helical structure of the parent sequence, and that the thermodynamic stability of the coiled coil depends on the position of the incorporation of the epsilon-residue. Crystal structures obtained for each peptide give insight into the chemical behavior and conformational preferences of the non-natural amino acid and show that the triazole ring can participate in the backbone hydrogen bonding of the alpha-helix as well as template an interhelical crossing between chains in the bundle.
About this Structure
Full crystallographic information is available from OCA.
Reference
Heterocyclic peptide backbone modifications in an alpha-helical coiled coil., Horne WS, Yadav MK, Stout CD, Ghadiri MR, J Am Chem Soc. 2004 Dec 1;126(47):15366-7. PMID:15563148 Page seeded by OCA on Sat May 3 10:55:56 2008
