1u9f: Difference between revisions

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[[Image:1u9f.~~jpg~~|left|200px]]

[[Image:1u9f.png|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)===

~~==Overview==~~

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_15563148}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15563148 is the PubMed ID number.

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==About this Structure==

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[[Category: Heterocycic backbone modification]]

[[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 Mon Jul 28 00:26:52 2008''

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-[[Image:1u9f.jpg|left|200px]]
+{{Seed}}
+[[Image:1u9f.png|left|200px]]
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 {{STRUCTURE_1u9f|  PDB=1u9f  |  SCENE=  }}
-'''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)===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15563148}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15563148 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15563148}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Heterocycic backbone modification]]
 [[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 Mon Jul 28 00:26:52 2008''