ChemPhysChem

Cover image for Vol. 12 Issue 3

Special Issue: Förster Resonance Energy Transfer

February 25, 2011

Volume 12, Issue 3

Pages 421–719

  1. Cover Picture

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorial
    5. Graphical Abstract
    6. News
    7. Reviews
    8. Minireviews
    9. Essay
    10. Communications
    11. Articles
    12. Preview
    1. Cover Picture: Improved Temporal Resolution and Linked Hidden Markov Modeling for Switchable Single-Molecule FRET (ChemPhysChem 3/2011) (page 421)

      Stephan Uphoff, Kristofer Gryte, Geraint Evans and Dr. Achillefs N. Kapanidis

      Version of Record online: 22 FEB 2011 | DOI: 10.1002/cphc.201190011

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      Theodor Förster, whose 100th birthday is celebrated in this special issue, first described and formalized Förster resonance energy transfer (FRET). FRET as a method provides unique information on biomolecular structure and dynamics, especially at the single-molecule level. The cover picture illustrates a recent extension to the single-molecule toolbox. Switchable FRET monitors multiple FRET pairs on the same molecule sequentially by switching acceptor fluorophores on and off. The two FRET pairs on one DNA molecule appear as distinct populations in a plot of FRET and donor–acceptor stoichiometry data. Optimized conditions as described by A. N. Kapanidis et al. on p. 571 improve the temporal resolution of the method by an order of magnitude. Furthermore, linked hidden Markov modeling analysis identifies transient FRET states and links them to the donor–acceptor stoichiometry.

  2. Inside Cover

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorial
    5. Graphical Abstract
    6. News
    7. Reviews
    8. Minireviews
    9. Essay
    10. Communications
    11. Articles
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    1. Inside Cover: Homo-FRET Imaging as a Tool to Quantify Protein and Lipid Clustering (ChemPhysChem 3/2011) (page 422)

      Dr. Arjen N. Bader, Dr. Sandra Hoetzl, Dr. Erik G. Hofman, Jarno Voortman, Dr. Paul M. P. van Bergen en Henegouwen, Prof. Dr. Gerrit van Meer and Prof. Dr. Hans C. Gerritsen

      Version of Record online: 22 FEB 2011 | DOI: 10.1002/cphc.201190012

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      Homo-FRET, Förster resonance energy transfer between identical fluorophores, can be employed in microscopy to quantify cluster sizes as well as cluster size distributions in cells, as shown by H. C. Gerritsen et al. on p. 475.

  3. Editorial

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorial
    5. Graphical Abstract
    6. News
    7. Reviews
    8. Minireviews
    9. Essay
    10. Communications
    11. Articles
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    1. You have free access to this content
      Theodor Förster: A Giant of Modern Photochemistry (pages 423–424)

      Dr. Clemens F. Kaminski, Prof. Dr. Erich Sackmann and Prof. Dr. Klaus Schulten

      Version of Record online: 22 FEB 2011 | DOI: 10.1002/cphc.201100041

  4. Graphical Abstract

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorial
    5. Graphical Abstract
    6. News
    7. Reviews
    8. Minireviews
    9. Essay
    10. Communications
    11. Articles
    12. Preview
  5. News

    1. Top of page
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    1. Improving Electronics (page 441)

      Version of Record online: 22 FEB 2011 | DOI: 10.1002/cphc.201100078

  6. Reviews

    1. Top of page
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    3. Inside Cover
    4. Editorial
    5. Graphical Abstract
    6. News
    7. Reviews
    8. Minireviews
    9. Essay
    10. Communications
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    1. How Förster Resonance Energy Transfer Imaging Improves the Understanding of Protein Interaction Networks in Cancer Biology (pages 442–461)

      Dr. Gilbert O. Fruhwirth, Dr. Luis P. Fernandes, Dr. Gregory Weitsman, Dr. Gargi Patel, Dr. Muireann Kelleher, Dr. Katherine Lawler, Adrian Brock, Dr. Simon P. Poland, Dr. Daniel R. Matthews, Prof. György Kéri, Dr. Paul R. Barber, Prof. Borivoj Vojnovic, Dr. Simon M. Ameer-Beg, Prof. Anthony C. C. Coolen, Dr. Franca Fraternali and Prof. Tony Ng

      Version of Record online: 15 FEB 2011 | DOI: 10.1002/cphc.201000866

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      Worth more than a thousand words: FRET imaging can contribute at various stages to delineate the function of the proteome. We describe the basic principles of FRET imaging and discuss advanced high-content and intravital FRET imaging techniques with a special focus on their integration with protein interaction networks (see graphic).

    2. FRET Microscopy in 2010: The Legacy of Theodor Förster on the 100th Anniversary of his Birth (pages 462–474)

      Dr. Yuansheng Sun, Horst Wallrabe, Soo-Ah Seo and Prof. Dr. Ammasi Periasamy

      Version of Record online: 29 DEC 2010 | DOI: 10.1002/cphc.201000664

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      The scientific impact of Theodor Förster (picture, left), who would have been 100 years old this year, is still evolving. Combining his quantitative approach of Förster resonance energy transfer (FRET) and state-of-the-art digital imaging techniques allows scientists to breach the resolution limits of light in light microscopy and deduce molecular distances of 1–10 nm (center). This review covers Förster's theory, the elements of and challenges to successful FRET microscopy, and the wide-ranging impact of FRET in the life sciences (right).

  7. Minireviews

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorial
    5. Graphical Abstract
    6. News
    7. Reviews
    8. Minireviews
    9. Essay
    10. Communications
    11. Articles
    12. Preview
    1. Homo-FRET Imaging as a Tool to Quantify Protein and Lipid Clustering (pages 475–483)

      Dr. Arjen N. Bader, Dr. Sandra Hoetzl, Dr. Erik G. Hofman, Jarno Voortman, Dr. Paul M. P. van Bergen en Henegouwen, Prof. Dr. Gerrit van Meer and Prof. Dr. Hans C. Gerritsen

      Version of Record online: 22 DEC 2010 | DOI: 10.1002/cphc.201000801

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      Clustering of proteins or lipids in, for example, membranes in cells can be quantitatively imaged using homo-FRET. Various methods based on fluorescence anisotropy to study this molecular scale (<5 nm) interactions are reviewed (see picture).

    2. FRET in Cell Biology: Still Shining in the Age of Super-Resolution? (pages 484–490)

      Dr. Hernán E. Grecco and Dr. Peter J. Verveer

      Version of Record online: 29 DEC 2010 | DOI: 10.1002/cphc.201000795

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      Super-resolution FRET: Fluorescence resonance energy transfer (FRET) microscopy is a powerful tool to detect biological interactions and activities in living cells. New developments in fluorescence microscopy now enable imaging of cellular structures with unprecedented spatial resolution. The possibilities for combining FRET with super-resolution microscopy are explored.

    3. Single-Molecule Fluorescence Coincidence Spectroscopy and its Application to Resonance Energy Transfer (pages 491–499)

      Dr. Angel Orte, Dr. Richard W. Clarke and Prof. David Klenerman

      Version of Record online: 4 OCT 2010 | DOI: 10.1002/cphc.201000636

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      Binocular vision adds depth: The use of single-molecule coincidence spectroscopy to study FRET systems, using one or two confocal lasers of different colours is described. The advantages of the coincidence spectroscopy are highlighted and illustrated with examples of its application to some biological systems of interest. The picture shows a TCCD–FRET application to RNA folding.

    4. HomoFRET Fluorescence Anisotropy Imaging as a Tool to Study Molecular Self-Assembly in Live Cells (pages 500–509)

      Fiona T. S. Chan, Dr. Clemens F. Kaminski and Dr. Gabriele S. Kaminski Schierle

      Version of Record online: 29 DEC 2010 | DOI: 10.1002/cphc.201000833

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      Fluorescence anisotropy imaging is reviewed as a tool to study protein self-assembly reactions in live cells. A summary is given of the current state-of-the-art and case studies are presented of successful implementations, highlighting technical aspects which have to be mastered to bridge the gap between proof-of-concept experiments and biological discoveries.

    5. Time-Dependent FRET with Single Enzymes: Domain Motions and Catalysis in H+-ATP Synthases (pages 510–517)

      Dr. Roland Bienert, Dr. Boris Zimmermann, Dr. Verena Rombach-Riegraf and Prof. Dr. Peter Gräber

      Version of Record online: 2 FEB 2011 | DOI: 10.1002/cphc.201000921

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      Molecular machines: H+-ATP synthases couple transmembrane proton transport with ATP synthesis from ADP and inorganic phosphate by a rotational mechanism. Single-pair fluorescence resonance energy transfer (spFRET) in single molecules is a powerful tool to analyse conformational changes (see picture). It is used to investigate subunit movements in H+-ATP synthases from E. coli (EF0F1) and from spinach chloroplasts (CF0F1) during catalysis.

    6. Förster Energy Transfer Theory as Reflected in the Structures of Photosynthetic Light-Harvesting Systems (pages 518–531)

      Dr. Melih Şener, Johan Strümpfer, Dr. Jen Hsin, Danielle Chandler, Dr. Simon Scheuring, Prof. C. Neil Hunter and Prof. Klaus Schulten

      Version of Record online: 22 FEB 2011 | DOI: 10.1002/cphc.201000944

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      Förster's theory of excitation transfer is summarized, including recent extensions, and the relevance of the theory to photosynthetic systems as evolved in purple bacteria (see picture), cyanobacteria, and plants is demonstrated.

    7. FRET and FCS—Friends or Foes? (pages 532–541)

      Dr. Harekrushna Sahoo and Prof. Petra Schwille

      Version of Record online: 9 FEB 2011 | DOI: 10.1002/cphc.201000776

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      FRET and FCS: This minireview describes two techniques, FRET and FCS (fluorescence correlation spectroscopy), which are commonly applied in biological sciences. Besides shedding light on the two methods by explaining their advantages and limitations, the authors focus on the combined application of FRET and FCS for exploring biological processes in a broader perspective (see picture).

      Corrected by:

      Corrigendum: Corrigendum: FRET and FCS—Friends or Foes?

      Vol. 12, Issue 4, 731, Version of Record online: 8 MAR 2011

    8. Improving FRET-Based Monitoring of Single Chemomechanical Rotary Motors at Work (pages 542–553)

      Dr. Michael Börsch and Prof. Dr. Jörg Wrachtrup

      Version of Record online: 8 FEB 2011 | DOI: 10.1002/cphc.201000702

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      Looking good! Single-molecule FRET studies of the membrane-embedded rotary nanomotor F0F1-ATP synthase are presented. Also, new ideas and concepts to overcome the current limitations of the confocal FRET detection approach are discussed, for example, nanodiamonds as new fluorophores, optimized laser excitation schemes, hidden Markov models or the anti-Brownian electrokinetic trap (ABELtrap, see picture).

  8. Essay

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorial
    5. Graphical Abstract
    6. News
    7. Reviews
    8. Minireviews
    9. Essay
    10. Communications
    11. Articles
    12. Preview
    1. The Scientific Work of Theodor Förster: A Brief Sketch of his Life and Personality (pages 555–558)

      Prof. Dr. Horst E. A. Kramer and Dr. Peter Fischer

      Version of Record online: 9 NOV 2010 | DOI: 10.1002/cphc.201000733

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      Out of the wealth of Theodor Förster's scientific work (see picture), three main research fields are discussed: 1) Förster resonance energy transfer (FRET), 2) the Förster cycle, linking protolysis and reprotonation of molecules in the excited state (in 1951 still considered unmeasurably fast), 3) excimer formation by association of, for example, an excited with an electronic-ground-state pyrene molecule.

  9. Communications

    1. Top of page
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    3. Inside Cover
    4. Editorial
    5. Graphical Abstract
    6. News
    7. Reviews
    8. Minireviews
    9. Essay
    10. Communications
    11. Articles
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    1. Light-Triggered Aggregation and Disassembly of Amyloid-Like Structures (pages 559–562)

      Andreas A. Deeg, Dr. Tobias E. Schrader, Susanne Kempter, Dr. Jose Pfizer, Prof. Dr. Luis Moroder and Prof. Dr. Wolfgang Zinth

      Version of Record online: 27 DEC 2010 | DOI: 10.1002/cphc.201001012

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      Switching amyloids by light: A light-switchable azobenzene peptide aggregates into amyloid-like structures when the azobenzene chromophore, incorporated as a backbone element, is in the trans form. The amyloids are disassembled by illumination which isomerizes the chromophore from trans to cis. The isomerized azobenzene forms a defect structure in the amyloids which leads to the disassembly of the aggregates within minutes.

    2. FRET Imaging by kt/kf (pages 563–566)

      Dr. M. Julia Roberti, Dr. Luciana Giordano, Dr. Thomas M. Jovin and Dr. Elizabeth A. Jares-Erijman

      Version of Record online: 27 JAN 2011 | DOI: 10.1002/cphc.201000925

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      A FRET formalism in terms of the ratio between the rate constants for deactivation of the donor excited state by resonance energy transfer (kt) and by emission (kf) is introduced (see picture). The advantages of the approach are illustrated by FRET imaging of the donor/acceptor system consisting of co-aggregates of the amyloid protein alpha-synuclein labeled with the biarsenical FlAsH and quantum dots (605 nm) functionalized with alpha-synuclein.

      Corrected by:

      Corrigendum: Corrigendum: FRET Imaging by kt/kf

      Vol. 12, Issue 6, 1033, Version of Record online: 8 APR 2011

    3. Emissive Nucleosides as Molecular Rotors (pages 567–570)

      Dr. Renatus W. Sinkeldam, Andrea J. Wheat, Hande Boyaci and Prof. Dr. Yitzhak Tor

      Version of Record online: 27 DEC 2010 | DOI: 10.1002/cphc.201001002

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      Sticky fingers: The emission intensity of modified pyrimidines containing an aryl moiety, linked by a single bond to the nucleobase in the 5-position, show a remarkable sensitivity to sample viscosity (see picture), a trait typical for chromophores bearing a molecular rotor element.

  10. Articles

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorial
    5. Graphical Abstract
    6. News
    7. Reviews
    8. Minireviews
    9. Essay
    10. Communications
    11. Articles
    12. Preview
    1. Improved Temporal Resolution and Linked Hidden Markov Modeling for Switchable Single-Molecule FRET (pages 571–579)

      Stephan Uphoff, Kristofer Gryte, Geraint Evans and Dr. Achillefs N. Kapanidis

      Version of Record online: 30 JAN 2011 | DOI: 10.1002/cphc.201000834

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      Optimized conditions for measuring the multiple distances within a single molecule by switchable FRET increase the temporal resolution of the method by an order of magnitude. Furthermore, linked Hidden Markov Modeling analysis identifies transient FRET states and links them to the donor–acceptor stoichiometry (see picture).

    2. Designing Dye–Nanochannel Antenna Hybrid Materials for Light Harvesting, Transport and Trapping (pages 580–594)

      Prof. Dr. Gion Calzaferri, Prof. Dr. Rachel Méallet-Renault, Dr. habil. Dominik Brühwiler, Dr. Robert Pansu, Dr. Igor Dolamic, Dr. Thomas Dienel, Pauline Adler, Prof. Dr. Huanrong Li and Dr. Andreas Kunzmann

      Version of Record online: 17 FEB 2011 | DOI: 10.1002/cphc.201000947

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      A photonic antenna for light harvesting and trapping is presented. The chromophores are embedded in the channels of the host. The green dyes act as donors which absorb the incoming light and transport the electronic excitation energy to the red acceptors located at the ends of the channels. The double arrows indicate the orientation of the electronic transition dipole moments.

    3. Energy Transfer Pathways in a Rylene-Based Triad (pages 595–608)

      Dr. Eduard Fron, Dr. Larissa Puhl, Dr. Ingo Oesterling, Dr. Chen Li, Prof. Dr. Klaus Müllen, Prof. Dr. Frans C. De Schryver, Prof. Dr. Johan Hofkens and Prof. Dr. Tom Vosch

      Version of Record online: 12 NOV 2010 | DOI: 10.1002/cphc.201000665

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      Rollercoaster energy: Excitation of the naphthalenemonoimide units in a rylene-based triad leads to efficient migration of the excitation energy towards the central terrylenediimide (see picture).

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      FLIM FRET Technology for Drug Discovery: Automated Multiwell-Plate High-Content Analysis, Multiplexed Readouts and Application in Situ (pages 609–626)

      Dr. Sunil Kumar, Dominic Alibhai, Dr. Anca Margineanu, Romain Laine, Dr. Gordon Kennedy, Dr. James McGinty, Sean Warren, Douglas Kelly, Dr. Yuriy Alexandrov, Dr. Ian Munro, Dr. Clifford Talbot, Dr. Daniel W. Stuckey, Dr. Christopher Kimberly, Dr. Bertrand Viellerobe, Dr. Francois Lacombe, Prof. Eric W.-F. Lam, Dr. Harriet Taylor, Prof. Margaret J. Dallman, Prof. Gordon Stamp, Dr. Edward J. Murray, Dr. Frank Stuhmeier, Dr. Alessandro Sardini, Prof. Matilda Katan, Dr. Daniel S. Elson, Prof. Mark A. A. Neil, Dr. Chris Dunsby and Prof. Paul M. W. French

      Version of Record online: 17 FEB 2011 | DOI: 10.1002/cphc.201000874

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      Chance of a lifetime: A fluorescence lifetime imaging (FLIM) technology platform to read out changes in Förster resonance energy transfer (FRET) efficiency is used for the study of protein interactions across the drug-discovery pipeline. An automated FLIM multiwell-plate reader acquires lifetime images of fixed and live cells labelled with fluorescent proteins in a few seconds per field of view (see picture) and can read a 96-well plate in less than 15 min.

    5. Evidence of a Folding Intermediate in RNase H from Single-Molecule FRET Experiments (pages 627–633)

      Robert Rieger, Dr. Andrei Kobitski, Dr. Hendrik Sielaff and Prof. Dr. G. Ulrich Nienhaus

      Version of Record online: 9 NOV 2010 | DOI: 10.1002/cphc.201000693

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      And then there were three: In previous single-molecule FRET data on RNase H, a typical three-state folder, only two states (folded/unfolded) could be distinguished at all GdmCl denaturant concentrations. The missing folding intermediate is now uncovered by fitting FRET efficiency histograms (see picture), measured with high statistical accuracy at many different GdmCl concentrations, by using a three-state model with globally constrained parameters.

    6. Davydov Splitting of Excitons in Cyclic Bacteriochlorophyll a Nanoaggregates of Bacterial Light-Harvesting Complexes between 4.5 and 263 K (pages 634–644)

      Mihkel Pajusalu, Dr. Margus Rätsep, Dr. Gediminas Trinkunas and Prof. Arvi Freiberg

      Version of Record online: 27 JAN 2011 | DOI: 10.1002/cphc.201000913

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      Exciting times for bacteria: The nature of electronic excitations created by photon absorption in the cyclic B850 aggregates of 18 bacteriochlorophyll molecules of LH2 antenna complexes of photosynthetic bacteria (see picture) is studied experimentally and theoretically over a broad temperature range using absorption, fluorescence, and fluorescence anisotropy spectra.

    7. A Mixed Quantum–Classical Description of Excitation Energy Transfer in Supramolecular Complexes: Förster Theory and beyond (pages 645–656)

      Jörg Megow, Prof. Dr. Beate Röder, Alexander Kulesza, Prof. Dr. Vlasta Bonačić-Koutecký and Dr. Volkhard May

      Version of Record online: 8 FEB 2011 | DOI: 10.1002/cphc.201000857

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      Mixing makes it possible: Electronic excitation energy transfer (EET) is described theoretically for the chromophore complex P4 formed by a butanediamine dendrimer to which four pheophorbide-a molecules are covalently linked (see picture). To achieve a description with atomic resolution, and to account for the effect of an ethanol solvent, a mixed quantum–classical methodology is utilized.

    8. Incorporating Multiple Energy Relay Dyes in Liquid Dye-Sensitized Solar Cells (pages 657–661)

      Dr. Jun-Ho Yum, Dr. Brian E. Hardin, Eric T. Hoke, Dr. Etienne Baranoff, Dr. Shaik M. Zakeeruddin, Dr. Mohammad K. Nazeeruddin, Prof. Tomas Torres, Prof. Michael D. McGehee and Prof. Michael Grätzel

      Version of Record online: 5 JAN 2011 | DOI: 10.1002/cphc.201000854

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      All the colours of the rainbow: Panchromatic response is essential to increase the light harvesting efficiency in solar conversion systems. The authors incorporate multiple energy relay dyes to gain a panchromatic response in dye-sensitized solar cells (see graphic). The complementary absorption spectrum due to Förster resonance energy transfer increases the photovoltaic performance by 35 %.

    9. Fluorescence Anisotropy of Molecular Rotors (pages 662–672)

      Dr. James A. Levitt, Pei-Hua Chung, Dr. Marina K. Kuimova, Dr. Gokhan Yahioglu, Yan Wang, Prof. Junle Qu and Dr. Klaus Suhling

      Version of Record online: 15 FEB 2011 | DOI: 10.1002/cphc.201000782

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      Fluorescent molecular rotors exhibit fluorescence lifetimes and quantum yields which are dependent on the viscosity of their surroundings. The fluorescence anisotropy of two molecular rotors has been compared with a rigid fluorophore by combining the Forster–Hoffmann equation with the Perrin equation. The steady-state anisotropy value gives a measure of intracellular viscosity via polarization-resolved fluorescence imaging (see picture).

    10. A FRET Sensor for Non-Invasive Imaging of Amyloid Formation in Vivo (pages 673–680)

      Dr. Gabriele S. Kaminski Schierle, Dr. Carlos W. Bertoncini, Fiona T. S. Chan, Annemieke T. van der Goot, Dr. Stefanie Schwedler, Dr. Jeremy Skepper, Dr. Simon Schlachter, Dr. Tjakko van Ham, Dr. Alessandro Esposito, Dr. Janet R. Kumita, Dr. Ellen A. A. Nollen, Prof. Christopher M. Dobson and Dr. Clemens F. Kaminski

      Version of Record online: 9 FEB 2011 | DOI: 10.1002/cphc.201000996

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      A novel sensor concept exploiting Förster resonance energy transfer to permit the aggregation kinetics of amyloidogenic proteins to be quantified in living systems is described. The sensor is enabled by the discovery that amyloid assemblies can act as energy acceptors for variants of fluorescent proteins. It is used to follow the kinetics of self-association reactions taking place in vitro and in vivo and reveal the nature of the ensuing aggregated species (see picture).

    11. Multiple Charge-Separation Pathways in Photosystem II: Modeling of Transient Absorption Kinetics (pages 681–688)

      Prof. Vladimir I. Novoderezhkin, Dr. Elisabet Romero, Prof. Jan P. Dekker and Prof. Dr. Rienk van Grondelle

      Version of Record online: 14 FEB 2011 | DOI: 10.1002/cphc.201000830

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      It happened so quickly: Modeling of transient absorption kinetics for isolated reaction centers of photosystem II shows that charge separation occurs from both the accessory chlorophyll and from the special pair (see picture).

    12. Single-Molecule FRET Ruler Based on Rigid DNA Origami Blocks (pages 689–695)

      Ingo H. Stein, Verena Schüller, Philip Böhm, Prof. Dr. Philip Tinnefeld and Prof. Dr. Tim Liedl

      Version of Record online: 9 FEB 2011 | DOI: 10.1002/cphc.201000781

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      FRET on a DNA origami structure: DNA origami assembly is used to position donor–acceptor pairs on the surface of DNA blocks for single-molecule energy transfer studies (see picture). In contrast to dsDNA FRET rulers, these origami blocks directly yield the expected distance dependence of energy transfer since the influence of the linkers on the donor–acceptor distance is reduced.

    13. Fluorescence Correlation Spectroscopy of Fast Chain Dynamics within Denatured Protein L (pages 696–703)

      Dr. Eilon Sherman and Prof. Dr. Gilad Haran

      Version of Record online: 26 JAN 2011 | DOI: 10.1002/cphc.201000722

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      Denatured but dynamic: The fluorescence of an oxazine dye labeling the C-terminus of denatured protein L is quenched upon contact with a tryptophan residue (violet). Measuring the dynamics of this quenching reaction by fluorescence correlation spectroscopy allows the authors to obtain the intrachain diffusion coefficient, which is surprisingly constant over a broad range of denaturant concentrations.

    14. Native and Unfolded States of Phosphoglycerate Kinase Studied by Single-Molecule FRET (pages 704–710)

      Tobias Rosenkranz, Dr. Ramona Schlesinger, Matteo Gabba and Dr. Jörg Fitter

      Version of Record online: 5 NOV 2010 | DOI: 10.1002/cphc.201000701

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      Molecular yoga: The two-domain protein PGK (see picture) shows a small but distinct compaction of the native state at low GndHCl concentrations. Even well above the unfolding transition (at C1/2=0.7 M GndHCl) PGK exhibits a progressive structural expansion with increasing denaturant concentrations.

    15. Fluorescence Blinking of the RC–LH1 Complex from Rhodopseudomonas palustris (pages 711–716)

      Sarah Unterkofler, Tobias Pflock, June Southall, Prof. Dr. Richard J. Cogdell and Prof. Dr. Jürgen Köhler

      Version of Record online: 22 OCT 2010 | DOI: 10.1002/cphc.201000588

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      Fluorescence intermittency: Blinking of individual RC–LH1 pigment-protein complexes (see picture) from the photosynthetic purple bacterium Rhodopseudomonas palustris is investigated. It is argued that the majority of the complexes reside in a prolonged on-state, due to a mechanism that is reminiscent of Coulomb blockade in semiconductor quantum dots.

  11. Preview

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorial
    5. Graphical Abstract
    6. News
    7. Reviews
    8. Minireviews
    9. Essay
    10. Communications
    11. Articles
    12. Preview
    1. You have free access to this content
      Preview: ChemPhysChem 4/2011 (page 719)

      Version of Record online: 22 FEB 2011 | DOI: 10.1002/cphc.201190015

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