IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v388y1997i6640d10.1038_41048.html
   My bibliography  Save this article

On/off blinking and switching behaviour of single molecules of green fluorescent protein

Author

Listed:
  • Robert M. Dickson

    (University of California San Diego)

  • Andrew B. Cubitt

    (†Aurora Biosciences)

  • Roger Y. Tsien

    (University of California San Diego)

  • W. E. Moerner

    (University of California San Diego)

Abstract

Optical studies of individual molecules at low and room temperature can provide information about the dynamics of local environments in solids, liquids and biological systems unobscured by ensemble averaging1,2,3,4,5,6,7,8,9,10,11,12,13,14. Here we present a study of the photophysical behaviour of single molecules of the green fluorescent protein (GFP) derived from the jellyfish Aequorea victoria. Wild-type GFP and its mutant have attracted interest as fluorescent biological labels because the fluorophore may be formed in vivo15,16. GFP mutants immobilized in aereated aqueous polymer gels and excited by 488-nm light undergo repeated cycles of fluorescent emission (‘blinking’) on a timescale of several seconds—behaviour that would be unobservable in bulk studies. Eventually the individual GFP molecules reach a long-lasting dark state, from which they can be switched back to the original emissive state by irradiation at 405 nm. This suggests the possibility of using these GFPs as fluorescent markers for time-dependent cell processes, and as molecular photonic switches or optical storage elements, addressable on the single-molecule level.

Suggested Citation

  • Robert M. Dickson & Andrew B. Cubitt & Roger Y. Tsien & W. E. Moerner, 1997. "On/off blinking and switching behaviour of single molecules of green fluorescent protein," Nature, Nature, vol. 388(6640), pages 355-358, July.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6640:d:10.1038_41048
    DOI: 10.1038/41048
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/41048
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/41048?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Paolo Annibale & Stefano Vanni & Marco Scarselli & Ursula Rothlisberger & Aleksandra Radenovic, 2011. "Quantitative Photo Activated Localization Microscopy: Unraveling the Effects of Photoblinking," PLOS ONE, Public Library of Science, vol. 6(7), pages 1-8, July.
    2. Omri Tau & Alice Henley & Anton N. Boichenko & Nadezhda N. Kleshchina & River Riley & Bingxing Wang & Danielle Winning & Ross Lewin & Ivan P. Parkin & John M. Ward & Helen C. Hailes & Anastasia V. Boc, 2022. "Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophore," Nature Communications, Nature, vol. 13(1), pages 1-7, December.
    3. Tatsuya Morisaki & James G McNally, 2014. "Photoswitching-Free FRAP Analysis with a Genetically Encoded Fluorescent Tag," PLOS ONE, Public Library of Science, vol. 9(9), pages 1-9, September.
    4. Anchal Srivastava & R K Shukla & Nishant Kumar & Anu Katiyar, 2017. "Nanoparticles as Biomarkers and Biosensors," Current Trends in Biomedical Engineering & Biosciences, Juniper Publishers Inc., vol. 9(3), pages 43-46, September.
    5. Atanu Maiti & Cosmo Z. Buffalo & Saumya Saurabh & Felipe Montecinos-Franjola & Justin S. Hachey & William J. Conlon & Geraldine N. Tran & Bakar Hassan & Kylie J. Walters & Mikhail Drobizhev & W. E. Mo, 2023. "Structural and photophysical characterization of the small ultra-red fluorescent protein," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:388:y:1997:i:6640:d:10.1038_41048. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.