This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1g04

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1g04.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1g04.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1g04| PDB=1g04 | SCENE= }}
{{STRUCTURE_1g04| PDB=1g04 | SCENE= }}
-
'''SOLUTION STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP PRION PROTEIN SEGMENT AND C-TERMINAL CYSTEINE'''
+
===SOLUTION STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP PRION PROTEIN SEGMENT AND C-TERMINAL CYSTEINE===
-
==Overview==
+
<!--
-
According to the "protein only" hypothesis, a conformational conversion of the non-pathogenic "cellular" prion isoform into a pathogenic "scrapie" isoform is the fundamental event in the onset of prion diseases. During this pathogenic conversion, helix H1 and two adjacent surface loops L2 and L3 of the normal prion protein are thought to undergo a conformational transition into an extended beta-like structure, which is prompted by interactions with the pre-existing beta-sheet. To get more insight into the interaction between the helix and one of the beta-strands in the partially unfolded prion protein, the solution structure of a synthetic linear peptide spanning helix H1 and beta-strand S2 (residues 142-166 in human numbering) was studied by circular dichroism and nuclear magnetic resonance spectroscopies. We found that, in contrast to many prion fragments studied earlier, this peptide (i) is highly soluble and does not aggregate up to a millimolar concentration range in aqueous medium and (ii) exhibits an intrinsic propensity to a beta-hairpin like conformation at neutral pH. This beta-propensity can be one of the internal driving forces of the molecular rearrangement responsible for the pathogenic conversion of the prion protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11577109}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11577109 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11577109}}
==About this Structure==
==About this Structure==
-
1G04 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G04 OCA].
+
1G04 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G04 OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: Beta hairpin]]
[[Category: Beta hairpin]]
[[Category: Prion]]
[[Category: Prion]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:57:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:12:04 2008''

Revision as of 01:12, 1 July 2008

Image:1g04.png

Template:STRUCTURE 1g04

SOLUTION STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP PRION PROTEIN SEGMENT AND C-TERMINAL CYSTEINE

Template:ABSTRACT PUBMED 11577109

About this Structure

1G04 is a Single protein structure. Full experimental information is available from OCA.

Reference

Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solution., Kozin SA, Bertho G, Mazur AK, Rabesona H, Girault JP, Haertle T, Takahashi M, Debey P, Hoa GH, J Biol Chem. 2001 Dec 7;276(49):46364-70. Epub 2001 Sep 27. PMID:11577109

Page seeded by OCA on Tue Jul 1 04:12:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g04"
Personal tools