1y32
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1y32.gif|left|200px]] | [[Image:1y32.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1y32", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | | | + | or leave the SCENE parameter empty for the default display. |
- | | | + | --> |
- | + | {{STRUCTURE_1y32| PDB=1y32 | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''NMR structure of humanin in 30% TFE solution''' | '''NMR structure of humanin in 30% TFE solution''' | ||
Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 1Y32 is a [[Single protein]] structure | + | 1Y32 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. |
==Reference== | ==Reference== | ||
Line 31: | Line 28: | ||
[[Category: Vlassi, M.]] | [[Category: Vlassi, M.]] | ||
[[Category: Zikos, C.]] | [[Category: Zikos, C.]] | ||
- | [[Category: | + | [[Category: Alzheimer's disease]] |
- | [[Category: | + | [[Category: Humanin]] |
- | [[Category: | + | [[Category: Neuroprotection]] |
- | [[Category: | + | [[Category: Nmr solution structure]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:49:33 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 12:49, 3 May 2008
NMR structure of humanin in 30% TFE solution
Overview
Humanin is a newly identified 24-residue peptide that suppresses neuronal cell death caused by a wide spectrum of familial Alzheimer's disease genes and the beta-amyloid peptide. In this study, NMR and circular dichroism studies of synthetic humanin in aqueous and 30% 2,2,2-trifluoroethanol (TFE) solutions are reported. In aqueous solution, humanin exists predominantly in an unstructured conformation in equilibrium with turn-like structures involving residues Gly5 to Leu10 and Glu15 to Leu18, providing indication of nascent helix. In the less polar environment of 30% TFE, humanin readily adopts helical structure with long-range order spanning residues Gly5 to Leu18. Comparative 3D modeling studies and topology predictions are in qualitative agreement with the experimental findings in both environments. Our studies reveal a flexible peptide in aqueous environment, which is free to interact with possible receptors that mediate its action, but may also acquire a helical conformation necessary for specific interactions and/or passage through membranes.
About this Structure
1Y32 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity., Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M, Biochem Biophys Res Commun. 2005 Apr 1;329(1):152-60. PMID:15721287 Page seeded by OCA on Sat May 3 15:49:33 2008