1qxc: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1qxc.jpg|left|200px]]
{{Seed}}
[[Image:1qxc.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qxc|  PDB=1qxc  |  SCENE=  }}  
{{STRUCTURE_1qxc|  PDB=1qxc  |  SCENE=  }}  


'''NMR structure of the fragment 25-35 of beta amyloid peptide in 20/80 v:v hexafluoroisopropanol/water mixture'''
===NMR structure of the fragment 25-35 of beta amyloid peptide in 20/80 v:v hexafluoroisopropanol/water mixture===




==Overview==
<!--
The design of molecules able to interact with the amyloid peptides either as inhibitors of fibril formation or as inhibitors of amyloid membrane pore formation represents one of the most relevant approaches in the development of anti-Alzheimer therapies. Abeta-(25-35), sequence GSNKGAIIGLM, is a highly toxic synthetic derivative of amyloid beta-peptides (Abeta-peptides), which forms fibrillary aggregates. Here, we report the NMR and CD investigation of Abeta-(25-35) in a membrane-mimicking environment and in isotropic mixtures of water and fluoro-alcohols to scan its conformational properties as a function of the medium. The analysis of the 3D structures in the mentioned conditions indicates a propensity of the peptide to behave as a typical transmembrane helix in the lipidic environment. In media characterized by different polarity, it loses the structural regularity at specific points of the sequence as a function of the environment. Furthermore, a comparison with the solution structure of full-length amyloid peptides suggests a role for the 25-27 kink region, which appears to be a general feature of all peptides under the solution conditions explored.
The line below this paragraph, {{ABSTRACT_PUBMED_15293994}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15293994 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15293994}}


==About this Structure==
==About this Structure==
1QXC is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXC OCA].  
1QXC is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXC OCA].  


==Reference==
==Reference==
Line 28: Line 32:
[[Category: Ursi, A M.D.]]
[[Category: Ursi, A M.D.]]
[[Category: Protein binding]]
[[Category: Protein binding]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:48:55 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:58:08 2008''

Revision as of 16:58, 28 July 2008

File:1qxc.png

Template:STRUCTURE 1qxc

NMR structure of the fragment 25-35 of beta amyloid peptide in 20/80 v:v hexafluoroisopropanol/water mixture

Template:ABSTRACT PUBMED 15293994

About this Structure

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

Reference

Solution structure of amyloid beta-peptide (25-35) in different media., D'Ursi AM, Armenante MR, Guerrini R, Salvadori S, Sorrentino G, Picone D, J Med Chem. 2004 Aug 12;47(17):4231-8. PMID:15293994

Page seeded by OCA on Mon Jul 28 19:58:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1qxc&oldid=713150"