Conformational Differences in Protein Disulfide Linkages Between Normal Hair and Hair From Subjects With Trichothiodystrophy: A Quantitative Analysis by Raman Microspectroscopy

    March 2006 in “ Biopolymers
    Sebastian Schlücker, Christine Liang, Katrin R. Strehle, John J. DiGiovanna, Kenneth H. Kraemer, Ira W. Levin
    TLDR TTD hair is brittle due to fewer sulfur amino acids and unstable disulfide bonds.
    The study used Raman microspectroscopy to analyze the disulfide linkages in hair from individuals with trichothiodystrophy (TTD) compared to normal hair. It found that TTD hair had a significant decrease in sulfur-containing amino acids and an increase in less stable disulfide conformers, specifically the gauche–gauche–trans (g-g-t) and trans–gauche–trans (t-g-t) forms. These conformational differences were suggested to contribute to the brittleness of hair observed in TTD. The findings were supported by quantum chemical calculations using density functional theory.
    Discuss this study in the Community →

    Research cited in this study

    2 / 2 results

    Related Community Posts Join

    0 / 0 results
    — no results

    Similar Research

    5 / 216 results