Spectroscopic detection of β -sheet structure in nascent Aβ oligomers
✍ Scribed by Mingjuan Wang; Renee D. JiJi
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 466 KB
- Volume
- 4
- Category
- Article
- ISSN
- 1864-063X
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Deep‐UV resonance Raman (UVRR) spectroscopy and circular dichroism (CD) were employed to study the secondary structure of Aβ(1–42) in fresh samples with increasing fractions of oligomeric peptide. A feature with a minimum at ∼217 nm appeared in CD spectra of samples containing oligomeric Aβ(1–42). UVRR spectra more closely resembled those of disordered proteins. The primary difference between UVRR spectra was the ratio of the 1236 cm^–1^ to 1260 cm^–1^ amide III peak intensities, which shifted in favor of the 1236 cm^–1^ band as the fraction of oligomeric peptide increased. (© 2011 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)
📜 SIMILAR VOLUMES
Amelogenins, a class of sparsely phosphorylated hydrophobic proteins characterized by a high concentration of Pro, Gln, Leu, and His have been implicated in the mineralization of tooth Recently a unique primary structure of bovine tooth enamel amelogenin was reported by Takagi et al.,3 characterized
## Abstract Self‐assembly of two tripeptide derivatives containing three nonpolar isoleucine moieties and polar oxyethylene groups are studied in methanol. Peptide __A__ [CH~3~(OCH~2~CH~2~)~3~OCH~2~CO(Ile)~3~OCH~3~] and peptide __B__ [CH~3~(OCH~2~CH~2~)~3~OCH~2~CO(Ile)~3~NH (CH~2~CH~2~O)~3~CH~3~] t
The stability of single -strands and multistrand -pleated sheets as elements of secondary structure is examined in the absence of intermolecular interactions. Such experimental conditions (e.g., complete removal of solvent molecules and counterions) are achieved by placing the peptide ions in the