1fb9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fb9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fb9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fb9| PDB=1fb9 | SCENE= }}
{{STRUCTURE_1fb9| PDB=1fb9 | SCENE= }}
-
'''EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN'''
+
===EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN===
-
==Overview==
+
<!--
-
Salmon calcitonin S-sulfonated analog (abbreviated as [S-SO(3)(-)]rsCT) was prepared by introducing two sulfonic groups into the side chains of Cys1 and Cys7 of recombinant salmon calcitonin. The hypocalcemic potency of this open-chain analog is 5500IU/mg, which is about 30% higher than that (4500IU/mg) of the wild type. The solution conformation of [S-SO(3)(-)]rsCT was studied in aqueous trifluoroethanol solution by CD, 2D-NMR spectroscopy, and distance geometry calculations. In the mixture of 60% TFE and 40% water, the peptide assumes an amphipathic alpha-helix in the region of residues 4-22, which is one turn longer than that of the native sCT. The structural feature analysis of the peptide revealed the presence of hydrophobic surface composed of five hydrophobic side chains of residues Leu4, Leu9, Leu12, Leu16, and Leu19, and a network of salt-bridges that consisted of a tetrad of oppositely charged side chains (Cys7-SO(3)(-)-Lys11(+)-Glu15(-)-Lys18(+)). The multiple salt bridges resulted in the stabilization of the longer amphipathic alpha-helix. Meanwhile, the higher hypocalcemic potency of the peptide could be attributed to the array of hydrophobic side chains of five leucine residues of the amphipathic alpha-helix.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12804605}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12804605 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12804605}}
==About this Structure==
==About this Structure==
-
1FB9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oncorhynchus_gorbuscha Oncorhynchus gorbuscha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FB9 OCA].
+
1FB9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oncorhynchus_gorbuscha Oncorhynchus gorbuscha]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FB9 OCA].
==Reference==
==Reference==
Line 27: Line 31:
[[Category: Wu, H.]]
[[Category: Wu, H.]]
[[Category: Alpha helix]]
[[Category: Alpha helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:07:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:59:25 2008''

Revision as of 23:59, 30 June 2008

Image:1fb9.png

Template:STRUCTURE 1fb9

EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN

Template:ABSTRACT PUBMED 12804605

About this Structure

1FB9 is a Single protein structure of sequence from Oncorhynchus gorbuscha. Full experimental information is available from OCA.

Reference

Solution structure and biological activity of recombinant salmon calcitonin S-sulfonated analog., Wang Y, Dou H, Cao C, Zhang N, Ma J, Mao J, Wu H, Biochem Biophys Res Commun. 2003 Jun 27;306(2):582-9. PMID:12804605

Page seeded by OCA on Tue Jul 1 02:59:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fb9"
Personal tools