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The analysis of merino wool cuticle and cortical cells by Fourier transform Raman spectroscopy
Author(s) -
Church Jeffrey S.,
Corino Gary L.,
Woodhead Andrea L.
Publication year - 1997
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199707)42:1<7::aid-bip2>3.0.co;2-s
Subject(s) - chemistry , raman spectroscopy , cuticle (hair) , cystine , amino acid , cysteine , fourier transform infrared spectroscopy , amide , keratin , crystallography , biophysics , biochemistry , chemical engineering , anatomy , biology , enzyme , paleontology , physics , optics , engineering
Wool fibers are comprised of proteins known as α‐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 Raman spectra of cortical and cuticle cells isolated from fine Merino wool fibers have been obtained. Raman spectroscopy has been shown to be sensitive to the differences in both secondary structure and amino acid composition. The cortical cells were found to be higher in α‐helical content as compared to the cuticle cells, which had an increased disordered content. Specific information, consistent with amino acid analysis results, regarding cystine, tyrosine, tryptophan, and phenylalanine residues, were obtained for both the cortical and cuticle cells. In addition, the Raman spectra provided information about free thiol groups, amino acids residues with amide group side chains, and residues with protonated carboxyl group side chains. Middle ir transmission spectra of these isolated cells were also obtained. In comparison to the Raman data, the middle ir spectra were found to be not as rich in information. © 1997 John Wiley & Sons, Inc. Biopoly 42: 7–17, 1997