A New Protein Conformation Indicator Based on Biarsenical Fluorescein with an Extended Benzoic Acid Moiety

DOI PDF Web Site Web Site Web Site View 1 Remaining Hide 32 References

Bibliographic Information

Other Title
  • New Protein Conformation Indicator Based on Biarsenical Fluorescein with an Extended Benzoic Acid Moiety

Search this article

Abstract

We demonstrate herein a new protein conformation indicator based on biarsenical fluorescein with an extended benzoic acid moiety. The present indicator is reactive to a genetically introduced tetracysteine motif (Cys-Cys-Xaa-Xaa-Cys-Cys, where Xaa is a noncysteine amino acid) of proteins. Compared to the original biarsenical fluorescein (FlAsH) and the biarsenical Nile red analogue (BArNile), the present indicator exhibited larger fluorescence intensity changes in response to Ca2+-induced conformational rearrangements of calmodulin. A calculation of the highest occupied molecular orbital (HOMO) level of the benzoic acid moiety of the indicator molecule supports possible involvement of a photoinduced electron transfer (PET) process. These results indicate that the present indicator is useful for sensitive detection of protein conformational changes.

Journal

  • Analytical Sciences

    Analytical Sciences 20 (2), 273-278, 2004

    The Japan Society for Analytical Chemistry

References(32)*help

See more

Keywords

Details 詳細情報について

Report a problem

Back to top