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Conformational differences in protein disulfide linkages between normal hair and hair from subjects with trichothiodystrophy: A quantitative analysis by Raman microspectroscopy

✍ Scribed by S. Schlücker; C. Liang; K. R. Strehle; J. J. DiGiovanna; K. H. Kraemer; I. W. Levin


Book ID
101722178
Publisher
Wiley (John Wiley & Sons)
Year
2006
Tongue
English
Weight
319 KB
Volume
82
Category
Article
ISSN
0006-3525

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✦ Synopsis


Abstract

Raman spectra of normal hair shafts and hair shafts from patients exhibiting trichothiodystrophy (TTD) were obtained using line focus laser illumination. Because hair from TTD patients has a significant decrease in the content of the sulfur‐containing amino acids in comparison to normal hair, the 550–500 cm^−1^ disulfide stretching mode region of the Raman spectrum was examined in detail. A quantitative spectral analysis demonstrates significant increases in the two energetically less favored gauche–gauche–trans (g‐g‐t) and trans–gauche–trans (t‐g‐t) forms. These observations suggest that the increased amounts of these less stable disulfide conformers are contributing factors to or associated with the hair brittleness observed for this congenital disorder. Structure–spectra correlations for the three dominant disulfide conformers are confirmed by quantum chemical calculations using modern density functional theory (DFT). © 2006 Wiley Periodicals, Inc. Biopolymers 82: 615–622, 2006

This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]