1j4m: Difference between revisions

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[[Image:1j4m.jpg|left|200px]]<br /><applet load="1j4m" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1j4m.jpg|left|200px]]<br /><applet load="1j4m" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1j4m" />

'''Minimized average structure of the 14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)'''<br />

==Overview==

Here we present a combinatorial approach to evolve a stable beta-hairpin, fold in a linear peptide. Starting with a de novo-designed linear peptide, that shows a beta-hairpin structure population of around 30%, we selected, four positions to build up a combinatorial library of 20(4) sequences., Deconvolution of the library using circular dichroism reduced such a, sequence complexity to 36 defined sequences. Circular dichroism and NMR of, these peptides resulted in the identification of two linear 14-aa-long, peptides that in plain buffered solutions showed a percentage of, beta-hairpin structure higher than 70%. Our results show how combinatorial, approaches can be used to obtain highly structured peptide sequences that, could be used as templates in which functionality can be introduced.

Here we present a combinatorial approach to evolve a stable beta-hairpin fold in a linear peptide. Starting with a de novo-designed linear peptide that shows a beta-hairpin structure population of around 30%, we selected four positions to build up a combinatorial library of 20(4) sequences. Deconvolution of the library using circular dichroism reduced such a sequence complexity to 36 defined sequences. Circular dichroism and NMR of these peptides resulted in the identification of two linear 14-aa-long peptides that in plain buffered solutions showed a percentage of beta-hairpin structure higher than 70%. Our results show how combinatorial approaches can be used to obtain highly structured peptide sequences that could be used as templates in which functionality can be introduced.

==About this Structure==

1J4M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1J4M OCA].

1J4M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4M OCA].

==Reference==

Line 13:

[[Category: Protein complex]]

[[Category: Lacroix, E.]]

[[Category: Pastor, M.T.]]

[[Category: Pastor, M T.]]

[[Category: Paz, M.Lopez.de.la.]]

[[Category: Paz, M Lopez de la.]]

[[Category: Perez-Paya, E.]]

[[Category: Serrano, L.]]

[[Category: beta-hairpin]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sat Nov 24 23~~:05:~~33 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:49 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1j4m.jpg|left|200px]]<br /><applet load="1j4m" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1j4m.jpg|left|200px]]<br /><applet load="1j4m" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1j4m" />
 '''Minimized average structure of the 14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)'''<br />
 ==Overview==
-Here we present a combinatorial approach to evolve a stable beta-hairpin, fold in a linear peptide. Starting with a de novo-designed linear peptide, that shows a beta-hairpin structure population of around 30%, we selected, four positions to build up a combinatorial library of 20(4) sequences., Deconvolution of the library using circular dichroism reduced such a, sequence complexity to 36 defined sequences. Circular dichroism and NMR of, these peptides resulted in the identification of two linear 14-aa-long, peptides that in plain buffered solutions showed a percentage of, beta-hairpin structure higher than 70%. Our results show how combinatorial, approaches can be used to obtain highly structured peptide sequences that, could be used as templates in which functionality can be introduced.
+Here we present a combinatorial approach to evolve a stable beta-hairpin fold in a linear peptide. Starting with a de novo-designed linear peptide that shows a beta-hairpin structure population of around 30%, we selected four positions to build up a combinatorial library of 20(4) sequences. Deconvolution of the library using circular dichroism reduced such a sequence complexity to 36 defined sequences. Circular dichroism and NMR of these peptides resulted in the identification of two linear 14-aa-long peptides that in plain buffered solutions showed a percentage of beta-hairpin structure higher than 70%. Our results show how combinatorial approaches can be used to obtain highly structured peptide sequences that could be used as templates in which functionality can be introduced.
 ==About this Structure==
-J4M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J4M OCA].
+J4M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4M OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Lacroix, E.]]
-[[Category: Pastor, M.T.]]
+[[Category: Pastor, M T.]]
-[[Category: Paz, M.Lopez.de.la.]]
+[[Category: Paz, M Lopez de la.]]
 [[Category: Perez-Paya, E.]]
 [[Category: Serrano, L.]]
 [[Category: beta-hairpin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:05:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:49 2008''