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.
1y32
From Proteopedia
|
NMR structure of humanin in 30% TFE solution
Contents |
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.
Disease
Known disease associated with this structure: Hartnup disorder OMIM:[608893]
About this Structure
1Y32 is a Single protein structure of sequence from [1]. 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 Mon Nov 12 20:14:18 2007
