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.
1skh
From Proteopedia
(New page: 200px<br /><applet load="1skh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1skh" /> '''N-terminal (1-30) of bovine Prion protein'''...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1skh.gif|left|200px]]<br /><applet load="1skh" size=" | + | [[Image:1skh.gif|left|200px]]<br /><applet load="1skh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1skh" /> | caption="1skh" /> | ||
'''N-terminal (1-30) of bovine Prion protein'''<br /> | '''N-terminal (1-30) of bovine Prion protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure and membrane interaction of the N-terminal sequence (1-30) | + | The structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein (bPrPp) has been investigated by NMR spectroscopy in phospholipid membrane mimetic systems. CD spectroscopy revealed that the peptide adopts a largely alpha-helical structure in zwitterionic bicelles as well as in DHPC micelles but has a less degree of alpha-helix structure in partly charged bicelles. The solution structure of bPrPp was determined in DHPC micelles, and an alpha-helix was found between residues Ser8 and Ile21. The residues within the helical region show slow amide hydrogen exchange. Translational diffusion measurements in zwitterionic q = 0.5 bicelles show that the peptide does not induce aggregation of the bicelles. Increased quadrupolar splittings were observed in the outer part of the (2)H spectrum of DMPC in q = 3.5 bicelles, indicating that the peptide induces a certain degree of order in the bilayer. The amide hydrogen exchange and the (2)H NMR results are consistent with a slight positive hydrophobic mismatch and that bPrPp forms a stable helix that inserts in a transmembrane location in the bilayer. The structure of bPrPp and its position in the membrane may be relevant for the understanding of how the N-terminal (1-30) part of the bovine PrP functions as a cell-penetrating peptide. These findings may lead to a better understanding of how the prion protein accumulates at the membrane surface and also how the conversion into the scrapie form is carried out. |
==About this Structure== | ==About this Structure== | ||
| - | 1SKH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1SKH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SKH OCA]. |
==Reference== | ==Reference== | ||
| Line 19: | Line 19: | ||
[[Category: coil-helix-coil]] | [[Category: coil-helix-coil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:25 2008'' |
Revision as of 13:02, 21 February 2008
|
N-terminal (1-30) of bovine Prion protein
Overview
The structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein (bPrPp) has been investigated by NMR spectroscopy in phospholipid membrane mimetic systems. CD spectroscopy revealed that the peptide adopts a largely alpha-helical structure in zwitterionic bicelles as well as in DHPC micelles but has a less degree of alpha-helix structure in partly charged bicelles. The solution structure of bPrPp was determined in DHPC micelles, and an alpha-helix was found between residues Ser8 and Ile21. The residues within the helical region show slow amide hydrogen exchange. Translational diffusion measurements in zwitterionic q = 0.5 bicelles show that the peptide does not induce aggregation of the bicelles. Increased quadrupolar splittings were observed in the outer part of the (2)H spectrum of DMPC in q = 3.5 bicelles, indicating that the peptide induces a certain degree of order in the bilayer. The amide hydrogen exchange and the (2)H NMR results are consistent with a slight positive hydrophobic mismatch and that bPrPp forms a stable helix that inserts in a transmembrane location in the bilayer. The structure of bPrPp and its position in the membrane may be relevant for the understanding of how the N-terminal (1-30) part of the bovine PrP functions as a cell-penetrating peptide. These findings may lead to a better understanding of how the prion protein accumulates at the membrane surface and also how the conversion into the scrapie form is carried out.
About this Structure
1SKH is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein., Biverstahl H, Andersson A, Graslund A, Maler L, Biochemistry. 2004 Nov 30;43(47):14940-7. PMID:15554701
Page seeded by OCA on Thu Feb 21 15:02:25 2008
