1nay: Difference between revisions

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

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

caption="1nay, resolution 2.60Å" />

'''GPP-Foldon:X-ray structure'''<br />

==Overview==

In a designed fusion protein the trimeric domain foldon from bacteriophage, T4 fibritin was connected to the C terminus of the collagen model peptide, (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the, three-stranded collagen triple helix. Crystal structure analysis at 2.6 A, resolution revealed conformational changes within the interface of both, domains compared with the structure of the isolated molecules. A striking, feature is an angle of 62.5 degrees between the symmetry axis of the, foldon trimer and the axis of the triple helix. The melting temperature of, (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is, higher than that of isolated (GlyProPro)(10,) which suggests an entropic, stabilization compensating for the destabilization at the interface.

In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 A resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5 degrees between the symmetry axis of the foldon trimer and the axis of the triple helix. The melting temperature of (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is higher than that of isolated (GlyProPro)(10,) which suggests an entropic stabilization compensating for the destabilization at the interface.

==About this Structure==

1NAY 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=1NAY OCA].

1NAY 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=1NAY OCA].

==Reference==

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[[Category: collagen assembly]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sat Nov 24 22~~:51:~~55 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:11 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1nay.gif|left|200px]]<br /><applet load="1nay" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1nay.gif|left|200px]]<br /><applet load="1nay" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1nay, resolution 2.60&Aring;" />
 '''GPP-Foldon:X-ray structure'''<br />
 ==Overview==
-In a designed fusion protein the trimeric domain foldon from bacteriophage, T4 fibritin was connected to the C terminus of the collagen model peptide, (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the, three-stranded collagen triple helix. Crystal structure analysis at 2.6 A, resolution revealed conformational changes within the interface of both, domains compared with the structure of the isolated molecules. A striking, feature is an angle of 62.5 degrees between the symmetry axis of the, foldon trimer and the axis of the triple helix. The melting temperature of, (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is, higher than that of isolated (GlyProPro)(10,) which suggests an entropic, stabilization compensating for the destabilization at the interface.
+In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 A resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5 degrees between the symmetry axis of the foldon trimer and the axis of the triple helix. The melting temperature of (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is higher than that of isolated (GlyProPro)(10,) which suggests an entropic stabilization compensating for the destabilization at the interface.
 ==About this Structure==
-NAY 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=1NAY OCA].
+NAY 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=1NAY OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: collagen assembly]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:51:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:11 2008''