Quantitative fluorescence microscopy, Special issue of the Journal of the Royal Society Interface

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New: topics covered in this series have been published in a dedicated issue of the Journal of the Royal Society Interface. Click here for free access

Overview

The Laser Analytics Group is proud to announce the 1st Theodor Förster International Lecture series at the University of Cambridge comprising lectures by some of the world's most eminent scientists in biological fluorescence imaging. The series has been made possible through generous donations by leading industries serving the microscopy field and state-of-the-art technology will be showcased in sessions following the main presentation, to offer visitors "hands on experience" on latest technology. In addition, a series of journal clubs connected to the lecture topics will be organised to prime interest and focus debate on the lectures' topics. At the heart of the lecture series is the application of quantitative fluorescence microscopy techniques, which are revolutionising the way in which research is being performed in the biological sciences today.

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Programme

Workshops and practical demonstrations as well as journal clubs will be announced at a later date.

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Venues (see programme)

Lectures will take place at the following locations:

Sanger Building,
New Biochemistry Lecture Theatre
University of Cambridge,
Tennis Court Road,
Cambridge CB2 1QW,
map

or

CRUK
Cancer Research UK Cambridge Research Institute
Li Ka Shing Centre
Robinson Way
Cambridge, CB2 0RE
map

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Theodor Förster

The series is in memory of Prof. Theodor Förster (1910-1974) whose ground breaking discoveries in photochemistry led to the development of some of the most powerful techniques available today in the arsenal of biophysicists.

Throughout his career, Förster held positions at the universities of Frankfurt, Leipzig, Posen, Stuttgart and the Max Planck Institute for Biophysical Chemistry in Göttingen. His main discoveries related to studies on proton transfer, energy transfer and excimer formation in electronically excited molecules, and investigation of photosynthetic processes. Many of his discoveries form the basis of modern fluorescence techniques and his legacy is continuing to influence the life sciences to this day.

A number of his ideas had a profound impact on fluorescence microscopy. For instance, Förster discovered that pyrene exhibits a red-shifted emission spectrum at high concentration and demonstrated that this depends on excimer formation, i.e., the formation of molecular homo-dimers mediated by an excited state. This process is nowadays exploited to study membrane dynamics by excimer-formation imaging (Pitto et al., Biochem. J. 344:177-184). Earlier in his career, Förster studied changes in acidity of molecules upon excitation. His method of determining equilibrium rate changes is nowadays referred to as the "Förster cycle". The green fluorescent protein was the first protein in which these effects were observed (Weber et al., Proc. Natl. Acad. Sci. USA 96:6177) forming a basis for an explanation of its fluorescence properties.

The discovery for which Förster is most famous for is the development of the theory for electronic energy transfer, now known as Förster Resonance Energy Transfer (FRET). FRET is a common process in nature referring to non-radiative energy transfer from a donor- to an acceptor- molecule. Foerster recognised that through a sequence of such interactions, energy can "migrate" over certain distances, a fact that explained a longstanding puzzle in photosynthesis, which display much higher photoconversion efficiencies than could be explained without energy migration.

FRET is a medium range dipole-dipole interaction and a semiclassical theory that was developed by Förster allows the process to be quantified. If the acceptor molecule is fluorescent then FRET can be quantified experimentally by measuring the sensitised emission from the acceptor, upon excitation of the donor. This mode of FRET measurement is has led to to the somewhat misleading term Fluorescence Resonance Energy Transfer for FRET, although the process is not mediated by a radiative process (i.e. there is no "Fluorescence Resonance" involved).

Its usefulness for biology stems from the fortuitious fact that FRET occurs over length scales characteristic of protein dimensions, and its efficiency decreases with the 6th power of the inter-chromophore distance. FRET can be used for the quantitative detection of conformational changes in macromolecules and protein-protein interactions (Jares-Erijman and Jovin, Nat. Biotech. 21:1387) . With the discovery of fluorescent proteins, FRET gained enormous significance in biology permitting the study of molecular events occurring on the nanoscale directly in the living cell (Wouters, Contemp. Phys. 47:239).

This lecture series is a celebration of the ingenious advances that have been made in the optical and biological sciences and at their interface lies one of the most exciting and dynamic research fields of current time.

  • Förster T. Zwischenmolekulare Energiewanderung und Fluoreszenz, Ann. Physik 6(2):55, 1948
  • Förster T., Die pH-Abhaengigkeit der Fluoreszenz von Naphthalinderivaten, Z. Elektrochem. 54:42, 1950
  • Förster T. and Kasper K., Ein Konzentrationsumschlag der Fluoreszenz, Z. Elektrochem., 59:977, 1955
  • Förster T. Delocalized excitation and excitation transfer in, O. Sinanoglu, ed., Modern Quantum Chemistry, 1965
  • Porter G. Some reflections on the work of Theodor Förster, Naturwissenschaften. 63(5):207-11, 1976

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Podcasts

We have recorded the past lectures for your convenience. Please click on the lecture title to watch it. You do need to have the windows media player on your computer to be able to view it. If you don't have it you can download the media player here.

Index of lecture podcasts (file downloads, app. 10MB)

  • Prof. Gratton: Tracking protein-coated particles in 3D


  • Dr. Hanley: Spectrally resolved lifetime imaging


  • Prof. Gerritsen: In-vivo non-linear spectral imaging


  • Prof. Vojnovic: Clinical Applications of FRET and FLIM


  • Prof. So: High Throughput, High Content 3D Tissue Image Cytometry



    • If you have problems watching the movies, click here (streamed version).

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    Organisers

    Laser Analytics Group Chairs:
    Dr. Clemens Kaminski (General Chair)
    Laser Analytics group
    Dept. of Chemical Engineering
    cfk23_AT_cam.ac.uk
    Dr. Alessandro Esposito (Programme Chair)
    Laser Analytics group
    Dept. of Chemical Engineering
    ae275_AT_cam.ac.uk
    Cancer Research UK Dr. Stefanie Reichelt
    Cambridge Cancer Research Centre
    sr411_AT_cam.ac.uk
    Gurdon Institute Dr. Alex Sossick
    Gurdon Institute
    AJS17_AT_cam.ac.uk

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    Sponsors

    This event has been made possible through generous donations from several sponsors:

    Physics of Living Matter The Physics of Living Matter (PLM) initiative, Cambridge
    Scientific Volume Imaging Scientific Volume Imaging BV, Laapersveld 63, 1213 VB Hilversum, The Netherlands
    Picoquant PicoQuant GmbH, Rudower Chaussee 29 (IGZ), 12489 Berlin, Germany
    Lambert Instruments Lambert Instruments, Turfweg 4, 9313 TH Leutingewolde, The Netherlands
    Leica Microsystems Leica Microsystems, Ernst-Leitz-Strasse 17-37, 35578 Wetzlar, Germany
    Nikon Nikon UK Ltd., 380 Richmond Road, Kingston upon Thames, Surrey KT2 5PR, United Kingdom
    Olympus Olympus UK Ltd., 2-8 Honduras Street, London EC1Y 0TX, United Kingdom
    Prior Prior Scientific Instruments LTD, Fulbourn, Cambridge, CBI 5ET U.K.0, United Kingdom