Display Settings:


Send to:

Choose Destination
See comment in PubMed Commons below
Biophys J. 2001 Dec;81(6):3566-76.

Stratum corneum protein dynamics as evaluated by a spin-label maleimide derivative: effect of urea.

Author information

  • 1Instituto de Física, Universidade Federal de Goiás, Goiânia 74001-970, Brazil. alonso@fisufg.br


The stratum corneum (SC) protein dynamics in the sulfhydryl group regions was studied by electron paramagnetic resonance (EPR) spectroscopy of a covalently attached maleimide derivative spin label. A two-state model for the nitroxide described the coexistence of two spectral components in the EPR spectra. The so-called strongly immobilized component arises from a spin-label fraction with the nitroxide moiety hydrogen-bonded to protein (rigid structure) and the weakly immobilized component is provided by the spin labels with higher mobility (approximately 10 times greater) exposed to the aqueous environment. The relative populations between these two states are in thermodynamic equilibrium. The apparent energetic gain for the nitroxide to form a hydrogen bond with the backbone rather than to be dissolved in the local environment was approximately 10 kcal/mol in the temperature range of 2-30 degrees C and approximately 6 kcal/mol in the range of 30-70 degrees C. Urea treatment caused a drastic increase in the segmental motion of the polypeptide chains that was completely reversible by its removal. Our analyses also indicated that the urea induced unfolding of the SC proteins opening the thiol group cavities. This work can also be useful to improve the spectral analysis of site-directed spin-labeling, especially for a more quantitative description of the nitroxide side chain mobility.

[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for PubMed Central
    Loading ...
    Write to the Help Desk