2oon: Difference between revisions

Revision as of 06:54, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2oon.png

Template:STRUCTURE 2oon

Structure of Ala14-PYY in aqueous solutionStructure of Ala14-PYY in aqueous solution

Template:ABSTRACT PUBMED 17580866

About this StructureAbout this Structure

2OON is a Single protein structure of sequence from Sus scrofa. Full experimental information is available from OCA.

ReferenceReference

Probing the formation of stable tertiary structure in a model miniprotein at atomic resolution: determinants of stability of a helical hairpin., Neumoin A, Mares J, Lerch-Bader M, Bader R, Zerbe O, J Am Chem Soc. 2007 Jul 18;129(28):8811-7. Epub 2007 Jun 20. PMID:17580866

Page seeded by OCA on Tue Jul 29 06:54:26 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2oon.jpg|left|200px]]
+{{Seed}}
+[[Image:2oon.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2oon|  PDB=2oon  |  SCENE=  }}
-'''Structure of Ala14-PYY in aqueous solution'''
+===Structure of Ala14-PYY in aqueous solution===
-==Overview==
+<!--
-The minimal model system to study the basic principles of protein folding is the hairpin. The formation of beta-hairpins, which are the basic components of antiparallel beta-sheets, has been studied extensively in the past decade, but much less is known about helical hairpins. Here, we probe hairpin formation between a polyproline type-II helix and an alpha-helix as present in the natural miniprotein peptide YY (PYY). Both turn sequence and interactions of aromatic side chains from the C-terminal alpha-helix with the pockets formed by N-terminal Pro residues are shown by site-directed mutagenesis and solution NMR spectroscopy in different solvent systems to be important determinants of backbone dynamics and hairpin stability, suggesting a close analogy with some beta-hairpin structures. It is shown that multiple relatively weak contacts between the helices are necessary for the formation of the helical hairpin studied here, whereas the type-I beta-turn acts like a hinge, which through certain single amino acid substitutions is destabilized such that hairpin formation is completely abolished. Denaturation and renaturation of tertiary structure by temperature or cosolvents were probed by measuring changes of chemical shifts. Folding of PYY is both reversible and cooperative as inferred from the sigmoidal denaturation curves displayed by residues at the interface of the helical hairpin. Such miniproteins thus feature an important hallmark of globular proteins and should provide a convenient system to study basic aspects of helical hairpin folding that are complementary to those derived from studies of beta-hairpins.
+The line below this paragraph, {{ABSTRACT_PUBMED_17580866}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17580866 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17580866}}
 ==About this Structure==
-OON is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OON OCA].
+OON is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OON OCA].
 ==Reference==
@@ Line 30: / Line 34: @@
 [[Category: Peptide yy]]
 [[Category: Pyy]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:20:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:54:26 2008''