OSA's Digital Library

Applied Spectroscopy

Applied Spectroscopy

| PUBLISHED BY SAS — AVAILABLE FROM SAS AND OSA

  • Vol. 62, Iss. 5 — May. 1, 2008
  • pp: 525–535

Attenuated Total Reflection Fourier Transform Infrared Spectroscopy Analysis of Human Hair Fiber Structure

Donald J. Lyman and Paula Schofield

Applied Spectroscopy, Vol. 62, Issue 5, pp. 525-535 (2008)


View Full Text Article

Acrobat PDF (1364 KB)





Browse Journals / Lookup Meetings

Browse by Journal and Year


   


Lookup Conference Papers

Close Browse Journals / Lookup Meetings

Article Tools

Share
Citations
  • Export Citation/Save Click for help

Abstract

The structure of human hair was studied by attenuated total reflection Fourier transform infrared (ATR-FT-IR) spectroscopy. The use of Ge, ZnSe, and Si internal reflection elements, various incident light angles, and difference spectra allowed detailed analysis of the cuticle, cortex, and cuticle–cortex intercellular regions without physically or mechanically removing the cuticle of the hair fiber. The ATR-FT-IR data showed the cuticle to be composed of protein having predominately beta-sheet and disorder and beta-turn configurations. In contrast, the cortex spectra showed alpha-helical structures due to the presence of intermediate filaments of alpha keratin plus beta-sheet, beta-turn and disorder structures. In the cuticle–cortex interface region the protein structures were primarily disorder and beta-turn with small amounts of beta-sheet configurations. The spectral analyses are consistent with the general information on hair fiber structure proposed in the literature.

Virtual Issues
Vol. 3, Iss. 6 Virtual Journal for Biomedical Optics

Citation
Donald J. Lyman and Paula Schofield, "Attenuated Total Reflection Fourier Transform Infrared Spectroscopy Analysis of Human Hair Fiber Structure," Appl. Spectrosc. 62, 525-535 (2008)
http://www.opticsinfobase.org/as/abstract.cfm?URI=as-62-5-525


Sort:  Journal  |  Reset

References

References are not available for this paper.

Cited By

OSA is able to provide readers links to articles that cite this paper by participating in CrossRef's Cited-By Linking service. CrossRef includes content from more than 3000 publishers and societies. In addition to listing OSA journal articles that cite this paper, citing articles from other participating publishers will also be listed.

« Previous Article  |  Next Article »

OSA is a member of CrossRef.

CrossCheck Deposited