Wool fibers are comprised of proteins known as a-keratins and have a complex morphological structure. The major components of this structure, the cuticle and cortical cells, differ in the conformations of their peptide chains as well as their amino acid compositions. High quality Fourier transform R
Study of the structure transformation of wool fibers with Raman spectroscopy
✍ Scribed by Hongling Liu; Weidong Yu
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 381 KB
- Volume
- 103
- Category
- Article
- ISSN
- 0021-8995
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Raman spectroscopy and tensile tests were used to investigate the structure transformation of stretched wool fibers with stretching ratios up to 110%. The typical bands analyzed in this article included the amide I region, the amide III region, the CC skeletal vibration region, and the SS and CS bond vibration region. To investigate the variations of the crystallinity and orientation of the wool fibers, the density and birefringence of the fibers were also measured. The results showed that the secondary structure of the wool fibers was transformed from an α‐helical structure to a β‐pleated‐sheet structure during the early stage of stretching. When the fiber was stretched more than 80%, the mechanism of stretching mainly relied on the slippage of the peptides. Meanwhile, the pretreatment of the wool fibers with sodium bisulfite and the setting processing resulted in the reduction of the concentration of the SS bonds. The results for the density and birefringence showed that the degree of crystallinity of the wool fibers decreased, whereas the degree of orientation increased during the stretching. The tensile behavior of the stretched wool also supported the α→β microstructure transformation. The diameter results showed that the extent of slenderization was about 25.3% when the stretching ratio was 80%. © 2006 Wiley Periodicals, Inc. J Appl Polym Sci 103: 1–7, 2007
📜 SIMILAR VOLUMES
## Abstract The chemical and conformational structures of __Bombyx mori__ silk were studied with the complementary techniques of Fourier transform Raman spectroscopy and Fourier transform infrared spectroscopy. The Fourier transform Raman spectrum of silk showed strong bands for the photosensitive
## Abstract The Raman spectra of human IgG, IgM, and rabbit IgG in lyophilized form and solution are reported. The spectral results indicate that the predominant structure in these immunoglobulin proteins is the antiparallel β‐sheet. The Raman spectra have also been obtained of rabbit anti‐ovalbumi
## Abstract The surface‐enhanced Raman scattering (SERS) technique for Fourier transform Raman spectrometry is employed to reveal the chemical structure of biological aliphatic compounds consisting of folded, long aliphatic chains. The structural analysis is performed via the measurements of the ac
## Abstract To investigate the internal structure changes in virgin black human hair keratin fibers due to aging, the structure of cross‐sections at various depths of virgin black human hair (sections of new growth hair: 2 mm from the scalp) from a group of eight Japanese females in their twenties
Raman spectroscopy and ultraviolet resonance Raman spectroscopy are versatile methods for probing details of protein structure and dynamics in complex biological assemblies, including viruses. The information contained in the Raman spectrum of a virus is ordinarily interpreted on the basis of an und