ChemPhysChem

Cover image for ChemPhysChem

Special Issue: Biophysics

July 13, 2009

Volume 10, Issue 9-10

Pages 1321–1687

  1. Cover Picture

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    3. Inside Cover
    4. Graphical Abstract
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    6. Reviews
    7. Minireviews
    8. Communications
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    1. Cover Picture: Structure, Dynamics and Optical Properties of Fluorescent Proteins: Perspectives for Marker Development (ChemPhysChem 9-10/2009) (page 1321)

      G. Ulrich Nienhaus and Jörg Wiedenmann

      Version of Record online: 29 JUN 2009 | DOI: 10.1002/cphc.200990034

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      The cover picture displays the tentacles of the sea anemone Entacmaea quadricolor, a source of red fluorescent proteins. The 2-imino-5-(4-hydroxybenzylidene)-imidazolinone chromophore (upper right) resides in the center of an 11-stranded β-barrel (lower left). The spectral properties of the fluorescent proteins depend on the conformation of the chromophore and its interactions with the surrounding protein scaffold. In the animal, the proteins form tight dimers or tetramers. Protein engineering yielded monomeric variants with optimized performance as protein tags in live cell imaging applications. On page 1369, G. U. Nienhaus and J. Wiedenmann review the structural diversity of GFP-like proteins and discuss how structure and dynamics govern their optical properties and how they can be modified to create advanced marker proteins.

  2. Inside Cover

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    1. Inside Cover: Stable, Non-Destructive Immobilization of Native Nuclear Membranes to Micro-Structured PDMS for Single-Molecule Force Spectroscopy (ChemPhysChem 9-10/2009) (page 1322)

      Martina Rangl, Reinat Nevo, Ivan Liashkovich, Victor Shahin, Ziv Reich, Andreas Ebner and Peter Hinterdorfer

      Version of Record online: 29 JUN 2009 | DOI: 10.1002/cphc.200990035

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      The investigation of native nuclear pore complexes (NPCs) with single-molecule force spectroscopy requires stable and non-destructive attachment of the nuclear envelope. Modified, micro-structured PDMS turns out to be perfectly suited for membrane preparation as it preserves structure and function of the entire NPC, as shown on p. 1553 by A. Ebner et al.

  3. Graphical Abstract

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  4. News

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  5. Reviews

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    1. SERS Microscopy: Nanoparticle Probes and Biomedical Applications (pages 1344–1354)

      Sebastian Schlücker

      Version of Record online: 29 JUN 2009 | DOI: 10.1002/cphc.200900119

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      Microspectroscopic imaging: Surface-enhanced Raman scattering (SERS) microscopy is a novel method of vibrational microspectroscopic imaging for the selective detection of biomolecules in targeted research. This review summarizes current designs of nanoparticle-based SERS probes (see figure) and highlights first biomedical applications of SERS microscopy for protein localization ex and in vivo.

    2. Recent Advances in Solution NMR: Fast Methods and Heteronuclear Direct Detection (pages 1356–1368)

      Isabella C. Felli and Bernhard Brutscher

      Version of Record online: 21 MAY 2009 | DOI: 10.1002/cphc.200900133

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      NMR spectroscopy for the molecular life sciences: Two areas of recent active research [fast methods and direct detection of low-γ nuclei (see schematic)] are reviewed herein. These are powerful new tools for structural characterization of short-lived molecules, large and intrinsically unstructured proteins, paramagnetic systems, as well as for the study of molecular kinetic processes at atomic resolution.

  6. Minireviews

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    1. Structure, Dynamics and Optical Properties of Fluorescent Proteins: Perspectives for Marker Development (pages 1369–1379)

      G. Ulrich Nienhaus and Jörg Wiedenmann

      Version of Record online: 19 FEB 2009 | DOI: 10.1002/cphc.200800839

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      Glow in the dark: Fluorescent proteins of the GFP family (see picture) are key tools for life sciences research. Recent structure–dynamics–function studies have yielded new insights that aid in the rational development of advanced fluorescent marker proteins. These new markers should further extend the range of possible applications.

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      Nonlinear Optical Spectroscopy of Soft Matter Interfaces (pages 1380–1388)

      Sylvie Roke

      Version of Record online: 26 MAY 2009 | DOI: 10.1002/cphc.200900138

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      Molecular interfacial properties of colloidal soft matter systems (for example vesicle fusion, or particle synthesis) can be investigated without the need of planar model systems or fluorescent labelling. Exclusively observing chemical properties and changes in a molecular layer of a few molecular dimensions thick around a small particle adds a new dimension to the field of surface science (see figure).

    3. Fluorescence Quenching by Photoinduced Electron Transfer: A Reporter for Conformational Dynamics of Macromolecules (pages 1389–1398)

      Sören Doose, Hannes Neuweiler and Markus Sauer

      Version of Record online: 27 MAY 2009 | DOI: 10.1002/cphc.200900238

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      Macromolecular dynamics: A technique for probing conformational dynamics of biomolecules based on contact-induced fluorescence quenching is discussed. Photoinduced electron transfer can be used to monitor structural variations with single-molecule sensitivity on sub-nanometre length scales and with nanosecond temporal resolution (see figure).

    4. Deforming DNA: From Physics to Biology (pages 1399–1404)

      Chantal Prévost, Masayuki Takahashi and Richard Lavery

      Version of Record online: 2 JUN 2009 | DOI: 10.1002/cphc.200900253

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      DNA molecules do the twist: The DNA double helix is a remarkably adaptable molecule that can undergo major conformational rearrangements without being irreversibly damaged. Indeed, DNA deformation is an intrinsic feature of many biological processes. In this Minireview, the authors summarize recent advances in the study of DNA deformation. The picture shows five different conformations of the double helix of DNA.

    5. 110 Years of the Meyer–Overton Rule: Predicting Membrane Permeability of Gases and Other Small Compounds (pages 1405–1414)

      Andreas Missner and Peter Pohl

      Version of Record online: 9 JUN 2009 | DOI: 10.1002/cphc.200900270

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      The transport of gaseous compounds across biological membranes (see picture) is essential in all forms of life. In this Minireview, the authors discuss recently reported violations of the well-established Meyer–Overton rule for small molecules, including carboxylic acids and gases, and show that Meyer and Overton continue to rule.

    6. Limitations of Induced Folding in Molecular Recognition by Intrinsically Disordered Proteins (pages 1415–1419)

      Eszter Hazy and Peter Tompa

      Version of Record online: 21 MAY 2009 | DOI: 10.1002/cphc.200900205

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      Intrinsically disordered proteins exist and function without well-defined three-dimensional structures and are common in proteomes where they carry out essential functions. Herein, evidence for their lack of structure and the major functional benefits that this confers, are surveyed. An example is Tβ4, a sequence that is disordered until it binds to G-actin, when it adopts an ordered conformation (see picture).

  7. Communications

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    1. The Excited-State Lifetimes in a G⋅C DNA Duplex are Nearly Independent of Helix Conformation and Base-Pairing Motif (pages 1421–1425)

      Kimberly de La Harpe, Carlos E. Crespo-Hernández and Bern Kohler

      Version of Record online: 19 MAR 2009 | DOI: 10.1002/cphc.200900004

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      DNA photophysics: Femtosecond transient absorption experiments reveal that excited states produced by UV light in a duplex DNA oligonucleotide decay at essentially the same rate in B and Z helix conformers (see figure).

    2. Role of Excited States in Low-Energy Electron (LEE) Induced Strand Breaks in DNA Model Systems: Influence of Aqueous Environment (pages 1426–1430)

      Anil Kumar and Michael D. Sevilla

      Version of Record online: 23 MAR 2009 | DOI: 10.1002/cphc.200900025

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      Low-energy electrons (LEEs) interact with a DNA model system to create a variety of excited states. In the gas phase, dissociative (σ*) states are accessible by LEEs with energy <4 eV (see picture) and cause facile strand breaks through a dissociative electron attachment mechanism. However, under solvation these dissociative (σ*) states are blue-shifted and are less accessible to LEEs.

    3. Optical Second Harmonic Generation Chiral Spectroscopy (pages 1431–1434)

      Stijn Foerier, Irina A. Kolmychek, Oleg A. Aktsipetrov, Thierry Verbiest and Ventsislav K. Valev

      Version of Record online: 12 MAR 2009 | DOI: 10.1002/cphc.200900045

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      Chiral spectroscopic study: The intensities of second harmonic generation chiral spectroscopy are obtained from the dispersion of the nonlinear optical susceptibility components, as a function of wavelength for helicenbisquinone thin films (see figure). A single formalism fits all the data simultaneously, and the findings constitute an important milestone towards the development of a new experimental technique.

    4. Monoanion BH4 Can Stabilize Zwitterionic Glycine with Dihydrogen Bonds (pages 1435–1437)

      Shan Xi Tian, Hai-Bei Li and Jinlong Yang

      Version of Record online: 8 MAY 2009 | DOI: 10.1002/cphc.200900158

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      Unusual strength: In the complex glycine–BH4, unconventional dihydrogen bonds are predicted. An ultrashort dihydrogen bond B[BOND]H⋅⋅⋅H[BOND]N and a very strong interaction of about −41 kcal mol−1) are found in complex 3 (see structures), in which the zwitterionic glycine is stabilized with a big margin.

    5. Weakened Hydrogen Bonds in Water Confined between Lipid Bilayers: The Existence of a Long-Range Attractive Hydration Force (pages 1438–1441)

      Zoran Arsov, Michael Rappolt and Joze Grdadolnik

      Version of Record online: 22 MAY 2009 | DOI: 10.1002/cphc.200900185

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      Stronger or weaker H-bonds? H-bonds in interlamellar water in partially hydrated lipid multibilayers are stronger with respect to bulk water. In contrast, the authors show by ATR–FTIR spectroscopy that the H-bonds are weaker in multibilayers in excess water (see spectra). This finding is of biological relevance for water-mediated phenomena in membranes.

    6. First-Principles Quantum Calculations on the Infrared Spectrum and Vibrational Dynamics of the Guanine-Cytosine Base Pair (pages 1442–1444)

      Kiyoshi Yagi, Hideyuki Karasawa, So Hirata and Kimihiko Hirao

      Version of Record online: 6 MAY 2009 | DOI: 10.1002/cphc.200900234

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      Vibrational resonance plays a vital role in manifesting a broad infrared band (>300 cm−1) and ultrafast vibrational energy relaxation (<100 femtoseconds) of the intermolecular NH stretching vibrations (see spectra).

    7. The Dynamic Side of the Hofmeister Effect: A Single-Molecule Nanopore Study of Specific Complex Formation (pages 1445–1449)

      Philip A. Gurnev, Daniel Harries, V. Adrian Parsegian and Sergey M. Bezrukov

      Version of Record online: 5 JUN 2009 | DOI: 10.1002/cphc.200900312

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      Beyond measurements of equilibria: An α-hemolysin nanopore is used as a single-molecule sensor to follow the effects of different salts on the complexation reaction of γ-cyclodextrin and adamantane carboxylate (see picture). The kinetics underlying the dynamic equilibrium are studied to reveal qualitatively different dynamic actions of various cosolute salts.

    8. A Force-Spectroscopy-Based Single-Molecule Metal-Binding Assay (pages 1450–1454)

      Yi Cao, Kai Shih Er, Rakesh Parhar and Hongbin Li

      Version of Record online: 9 JUN 2009 | DOI: 10.1002/cphc.200900333

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      Quantifying metal-binding by force: A quantitative single-molecule force-spectroscopy-based assay is developed to measure the binding affinity of metal ions to proteins. The method uses the unfolding force of a protein as a direct probe to distinguish the apo and metal-ion-bound forms of that protein and quantify the partitioning between the two forms (see figure).

    9. Correlated Movement and Bending of Nucleic Acid Structures Visualized by Multicolor Single-Molecule Spectroscopy (pages 1455–1460)

      Britta Person, Ingo H. Stein, Christian Steinhauer, Jan Vogelsang and Philip Tinnefeld

      Version of Record online: 4 JUN 2009 | DOI: 10.1002/cphc.200900109

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      At the end of the rainbow… The structure and dynamics of three- and four- way DNA junctions are studied using triple alternating laser excitation. Steroid binding distorts the structure of three-way junctions with correlated bending of all branches towards a steeper pyramid (see picture). In four-way junctions, the dynamics of three distances are visualized simultaneously.

    10. Plasmonically Controlled Nucleic Acid Dehybridization with Gold Nanoprisms (pages 1461–1465)

      Matthew R. Jones, Jill E. Millstone, David A. Giljohann, Dwight S. Seferos, Kaylie L. Young and Chad A. Mirkin

      Version of Record online: 8 MAY 2009 | DOI: 10.1002/cphc.200900269

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      Remote release: Triangular gold nanoprisms convert 1064 nm laser irradiation into heat selectively to allow the dehybridization of oligonucleotide conjugated to their surface (see scheme). These conjugates show unprecedented morphological stability under hours of irradiation. Released nucleic acids are unharmed by this process and can be repeatedly dehybridized and sequestered under spatiotemporal control.

    11. One-Pot Fabrication of High-Quality InP/ZnS (Core/Shell) Quantum Dots and Their Application to Cellular Imaging (pages 1466–1470)

      Sahid Hussain, Nayoun Won, Jutaek Nam, Jiwon Bang, Hyokyun Chung and Sungjee Kim

      Version of Record online: 9 JUN 2009 | DOI: 10.1002/cphc.200900159

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      True colors: High-quality InP and InP/ZnS quantum dots (QDs) are obtained by means of a simple one-pot method in the presence of polyethylene glycol (PEG). Rapid and size-controlled reactions lead to highly crystalline and nearly monodisperse QDs at relatively low temperatures. The particles emit from cyan blue to far-red, and are successfully used in cellular imaging (see figure).

    12. Single-Molecule Mechanical Unfolding of Amyloidogenic β2-Microglobulin: The Force-Spectroscopy Approach (pages 1471–1477)

      B. Sorce, S. Sabella, M. Sandal, B. Samorì, A. Santino, R. Cingolani, R. Rinaldi and P. P. Pompa

      Version of Record online: 3 JUN 2009 | DOI: 10.1002/cphc.200900220

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      The recombinant production of a novel chimeric polyprotein is described. The new protein contains either wild-type β2-microglobulin (β2m) or its truncated variant (ΔN6 β2m) (see picture). Structural characterization is achieved by means of single-molecule force spectroscopy studies of specific β2m regions which could be involved in amyloidogenesis.

    13. Topography and Recognition Imaging of Protein-Patterned Surfaces Generated by AFM Nanolithography (pages 1478–1481)

      Rong Zhu, Andreas Ebner, Markus Kastner, Johannes Preiner, Stefan Howorka and Peter Hinterdorfer

      Version of Record online: 2 JUN 2009 | DOI: 10.1002/cphc.200900245

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      Native-protein nanolithography is combined with topography and recognition imaging to synergistically use AFM tips to write and image nanoscale protein patterns on a surface (see picture). The approach is validated with different feedback modes, using surface-bound biotinylated bovine serum albumin (BSA) protein and AFM tips carrying streptavidin.

  8. Articles

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    1. Analysis of Non-Covalent Bioconjugation of Colloidal Nanoparticles by Means of Atomic Force Microscopy and Data Clustering (pages 1483–1491)

      Jessica Irrgang, Jacqueline Ksienczyk, Vidmantas Lapiene and Christof M. Niemeyer

      Version of Record online: 25 MAR 2009 | DOI: 10.1002/cphc.200800693

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      AFM topography data of non-covalently assembled biomolecule–nanoparticle hybrids is examined by statistical cluster analysis (see figure). As exemplified for fluorescent-protein-modified quantum dots and DNA/protein-conjugated gold nanoparticles, this analytical approach provides insights into the formation of bioconjugate populations.

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      Optical Spectroscopic Methods for Probing the Conformational Stability of Immobilised Enzymes (pages 1492–1499)

      Ashok Ganesan, Barry D. Moore, Sharon M. Kelly, Nicholas C. Price, Olaf J. Rolinski, David J. S. Birch, Ian R. Dunkin and Peter J. Halling

      Version of Record online: 9 APR 2009 | DOI: 10.1002/cphc.200800759

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      Structure of immobilised enzymes: Circular dichroism, infrared and fluorescence spectroscopic methods are used to characterise in situ structural stability of enzymes immobilised on particles. The enzyme subtilisin Carlsberg exhibits a similar secondary structure in solution and in the immobilised state but on the surface of porous silica gel a rigid tertiary structure is preferred (see picture).

    3. Conformational Preferences of the Full Chicken Prion Protein in Solution and Its Differences with Respect to Mammals (pages 1500–1510)

      Adriana Pietropaolo, Luca Muccioli, Claudio Zannoni and Enrico Rizzarelli

      Version of Record online: 2 JUN 2009 | DOI: 10.1002/cphc.200900078

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      Chicken nugget: Simulations of the full chicken prion protein (see picture) and chirality analysis provide possible explanations for its resistance to proteases—and for the fold stability of the avian prion globular core. The three alpha helices exhibit different flexibilities and secondary structure propensities.

    4. Probing Dynein and Kinesin Stepping with Mechanical Manipulation in a Living Cell (pages 1511–1516)

      Peter A. Sims and X. Sunney Xie

      Version of Record online: 5 JUN 2009 | DOI: 10.1002/cphc.200900113

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      Molecular motors: By combining optical tweezers and high-speed particle tracking, individual steps of microtubule motor proteins transporting organelles can be detected under known force loads in living mammalian cells (see figure).

    5. Site-Dependent Excited-State Dynamics of a Fluorescent Probe Bound to Avidin and Streptavidin (pages 1517–1532)

      Alexandre Fürstenberg, Oksana Kel, Julieta Gradinaru, Thomas R. Ward, Daniel Emery, Guillaume Bollot, Jiri Mareda and Eric Vauthey

      Version of Record online: 29 JUN 2009 | DOI: 10.1002/cphc.200900132

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      Sensing protein environment: The femtosecond fluorescence dynamics of a molecular probe attached to avidin and streptavidin (see figure) depends markedly on the location of the probe and on the protein. These differences reflect not only the protein primary and tertiary structures but also the effect of the surrounding water molecules.

    6. Characterization of the Biomechanical Properties of T4 Pili Expressed by Streptococcus pneumoniae—A Comparison between Helix-like and Open Coil-like Pili (pages 1533–1540)

      Mickaël Castelain, Efstratios Koutris, Magnus Andersson, Krister Wiklund, Oscar Björnham, Staffan Schedin and Ove Axner

      Version of Record online: 29 JUN 2009 | DOI: 10.1002/cphc.200900195

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      Adhesion strategies: Open coil-like T4 pili use different adhesion strategies in the presence of external forces (see figure) compared to the helix-like P pili. When exposed to significant forces, bacteria expressing helix-like pili remain attached by distributing the external force among a multitude of pili, whereas bacteria expressing open coil-like pili sustain large forces primarily by their multitude of binding adhesins.

    7. Detecting Sequential Bond Formation Using Three-Dimensional Thermal Fluctuation Analysis (pages 1541–1547)

      Tobias F. Bartsch, Samo Fišinger, Martin D. Kochanczyk, Rongxin Huang, Alexandr Jonáš and Ernst-Ludwig Florin

      Version of Record online: 22 MAY 2009 | DOI: 10.1002/cphc.200900211

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      Detecting specific bond formation: The formation of specific bonds between a particle and a substrate results in an immobilization of the particle that occurs in discrete steps, even for nanometer-sized complexes. Each configuration of bonds corresponds to a characteristic distribution of the particle's thermal position fluctuations (see picture).

    8. Coarse-Grain Simulations of the R-SNARE Fusion Protein in its Membrane Environment Detect Long-Lived Conformational Sub-States (pages 1548–1552)

      Marie-Pierre Durrieu, Peter J. Bond, Mark S. P. Sansom, Richard Lavery and Marc Baaden

      Version of Record online: 28 MAY 2009 | DOI: 10.1002/cphc.200900216

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      The detected conformational sub-states of an R-SNARE peptide inserted in a lipid bilayer (see figure) give insights into the membrane fusion mechanism. The simulations are in agreement with most experimental data on the SNARE system, but differ in some details that may have a functional interest. Comparing rat and yeast sequences shows some minor differences in their behaviour.

    9. Stable, Non-Destructive Immobilization of Native Nuclear Membranes to Micro-Structured PDMS for Single-Molecule Force Spectroscopy (pages 1553–1558)

      Martina Rangl, Reinat Nevo, Ivan Liashkovich, Victor Shahin, Ziv Reich, Andreas Ebner and Peter Hinterdorfer

      Version of Record online: 8 JUN 2009 | DOI: 10.1002/cphc.200900219

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      Stable anchorage: Micro-structured polydimethylsiloxane serves as an optimal specimen-support for immobilizing native nuclear membranes. It offers a solid basis for studying single-molecule interaction of proteins involved in nucleocytoplasmatic transport (see figure).

    10. Impact of External Stimuli and Cell Micro-Architecture on Intracellular Transport States (pages 1559–1566)

      Jean Mahowald, Delphine Arcizet and Doris Heinrich

      Version of Record online: 8 JUN 2009 | DOI: 10.1002/cphc.200900226

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      Unraveling the fast and complex processes involved in intracellular transport: Herein, the authors use a rolling-window analysis with very high temporal resolution to dissect the trajectory of an intracellular tracer and isolate transient active states (see graph). This is a signature of the activity which characterizes living materials.

    11. A Novel Heavy-Atom Label for Side-Specific Peptide Iodination: Synthesis, Membrane Incorporation and X-ray Reflectivity (pages 1567–1576)

      Philipp E. Schneggenburger, André Beerlink, Brigitte Worbs, Tim Salditt and Ulf Diederichsen

      Version of Record online: 29 JUN 2009 | DOI: 10.1002/cphc.200900241

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      A novel iodine peptide label for X-ray analysis of membrane-active peptide structures is applied to solid-phase peptide synthesis. The resulting pore-structured labeled peptide as well as a non-labeled reference were reconstituted in lipid bilayer stacks (see scheme). The results indicate the exhibition of a membrane-spanning β5.6-double helical peptide structure and illustrate the quality of the new label.

    12. Non-Random Distribution of Interleukin Receptors on the Cell Surface (pages 1577–1585)

      Attila Jenei, József Kormos, Gergely Szentesi, Adrienn J. Veres, Sándor Varga, Andrea Bodnár, Sándor Damjanovich and László Mátyus

      Version of Record online: 9 JUN 2009 | DOI: 10.1002/cphc.200900242

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      Spot the dots: Spatial organization of cell surface proteins plays a key role in the process of transmembrane signalling. Receptor clustering and changes in their cell surface distribution are often determining factors in the final outcome of ligand–receptor interactions. Herein, the authors show the applicability of Ripley's K(t) with additional algorithms a tool for analyzing the cell surface receptor patterns (see picture).

    13. Theory of Long-Range Diffusion of Proteins on a Spherical Biological Membrane: Application to Protein Cluster Formation and Actin-Comet Tail Growth (pages 1586–1592)

      Christian Amatore, Alexander I. Oleinick, Oleksiy V. Klymenko and Irina Svir

      Version of Record online: 27 MAY 2009 | DOI: 10.1002/cphc.200900176

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      Diffusional recruitment of proteins: Classical Brownian motion analysis describes the long-range movements of biomolecules on a spherical biological membrane. This protein diffusion process is prerequisite for the assembly of proteins which then cooperatively catalyze the polymerization of actin monomers to sustain the growth of actin tails (see picture).

    14. Diffusion with Moving Boundary on Spherical Surfaces (pages 1593–1602)

      Christian Amatore, Oleksiy V. Klymenko, Alexander I. Oleinick and Irina Svir

      Version of Record online: 8 JUN 2009 | DOI: 10.1002/cphc.200900169

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      Coming together: Surface diffusion of particles over a sphere and their clustering (see picture) may be adequately modelled by means of Brownian motion simulations or by using continuous Fick's diffusion law with a moving boundary in the low-concentration limit.

    15. Reinterpretation of the UV Spectrum of Cytosine: Only Two Electronic Transitions? (pages 1603–1606)

      Attila Tajti, Géza Fogarasi and Péter G. Szalay

      Version of Record online: 28 MAY 2009 | DOI: 10.1002/cphc.200900244

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      UV vibronic spectrum for cytosine has been calculated using high-level quantum chemistry. Coupled with a careful analysis of the available experimental spectra, it is suggested that the spectrum contains only two π–π* transitions; the other two, less resolved bands cannot be type π–π*, and are probably not even n–π* but rather vibrational subbands (see figure).

    16. Two-Color Two-Photon Excitation of Intrinsic Protein Fluorescence: Label-Free Observation of Proteolytic Digestion of Bovine Serum Albumin (pages 1607–1613)

      Stefan Quentmeier, Claudia C. Quentmeier, Peter J. Walla  and Karl-Heinz Gericke

      Version of Record online: 20 JAN 2009 | DOI: 10.1002/cphc.200800586

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      Two into one: Simultaneous absorption of two photons of different colors (2c2p) extends the applicable wavelength range of the Ti:Sa laser beyond that of conventional two-photon excitation (TPE) into the UV region (see schematic). The intrinsic fluorescence of bovine serum albumin during proteolytic cleavage by subtilisin (see plot) are monitored without exposing the protein to damaging UV radiation.

    17. Dynamics of gonococcal type IV pili during infection (pages 1614–1618)

      Dirk Opitz, Martin Clausen and Berenike Maier

      Version of Record online: 5 MAR 2009 | DOI: 10.1002/cphc.200800654

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      Keep that motor running: Type IV pili are among the strongest molecular motors characterized to date. Herein it is reported that pilus motors of the human pathogen Neisseria gonorrhoeae are very active for at least one day post-infection of epithelial cells. They generate force in the range on 70 pN and retract at a higher velocity as compared to abiotic environments (see picture).

    18. Electron-Capture-Induced Dissociation of Microsolvated Di- and Tripeptide Monocations: Elucidation of Fragmentation Channels from Measurements of Negative Ions (pages 1619–1623)

      Henning Zettergren, Lamri Adoui, Virgile Bernigaud, Henrik Cederquist, Nicole Haag, Anne I. S. Holm, Bernd A. Huber, Preben Hvelplund, Henrik Johansson, Umesh Kadhane, Mikkel Koefoed Larsen, Bo Liu, Bruno Manil, Steen Brøndsted Nielsen, Subhasis Panja, Jimmy Rangama, Peter Reinhed, Henning T. Schmidt and Kristian Støchkel

      Version of Record online: 5 MAR 2009 | DOI: 10.1002/cphc.200800782

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      The branching ratio between ammonia loss and N[BOND]Cα bond cleavage of singly charged microsolvated peptides after electron capture from cesium depends on the solvent molecule attached. Density functional calculations reveal that for [GA+H]+(CE) (G=glycine, A=alanine, CE=crown ether), the singly occupied molecular orbital of the neutral radical is located mainly on the amide group (see picture).

    19. Influence of Polyelectrolyte on DNA–RecA Nucleoprotein Filaments: Poly-L-Lysine Used as a Model (pages 1624–1629)

      Cunlan Guo, Gaiping Li, Zhelin Liu, Lanlan Sun, Yujing Sun, Fugang Xu, Yue Zhang, Tao Yang and Zhuang Li

      Version of Record online: 9 JUN 2009 | DOI: 10.1002/cphc.200800850

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      The effects of polyelectrolyte on the interaction of RecA protein and DNA are investigated in vitro by agarose gel electrophoresis and atomic force microscopy (see figure). Through changing the concentration, the length, and the addition orders of the polyelectrolyte, its effects on the DNA–RecA filaments are investigated and the probable mechanism is deduced.

    20. Structural Characterization by IRMPD Spectroscopy and DFT Calculations of Deprotonated Phosphorylated Amino Acids in the Gas Phase (pages 1630–1641)

      D. Scuderi, C. F. Correia, O. P. Balaj, G. Ohanessian, J. Lemaire and P. Maitre

      Version of Record online: 3 APR 2009 | DOI: 10.1002/cphc.200800856

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      Spectral assignment of the IRMPD bands and identification of the vibrational signatures of deprotonated phosphorylated amino acids are attained. The H2PO4 anion is used as a simple model of a free deprotonated phosphate group to identify the IR signatures of phosphorylation. The fragmentation efficiency is lower for [pSer-H] (left scale in figure) than for [pThr-H] and [pTyr-H] (right scale).

    21. Cysteine Oxidation by the Superoxide Radical: A Theoretical Study (pages 1642–1648)

      Bruno Cardey and Mironel Enescu

      Version of Record online: 30 MAR 2009 | DOI: 10.1002/cphc.200900010

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      Active molecular environment: Oxidation of the cysteine residue by the superoxide radical (see picture) is studied in the gas phase and in aqueous solution using the integrated molecular orbital+molecular orbital. It is shown that the molecular environment plays an important role in the oxidation of biologically relevant thiol compounds by the superoxide radical.

    22. Interaction of Cytidine 5′-Monophosphate with Au(111): An In Situ Infrared Spectroscopic Study (pages 1649–1655)

      Thomas Doneux and Lukáš Fojt

      Version of Record online: 3 APR 2009 | DOI: 10.1002/cphc.200900018

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      Attracted to gold: The interaction of cytidine 5′-monophosphate (CMP) with gold surfaces is studied at the Au(111) | aqueous solution interface. In situ infrared spectroscopy studies show that cytidine 5′-monophosphate is chemisorbed on Au(111) through the N3 atom of the pyrimidine ring (see picture).

    23. Targeted 13C–13C Distance Measurements in a Microcrystalline Protein via J-Decoupled Rotational Resonance Width Measurements (pages 1656–1663)

      Patrick C. A. van der Wel , Matthew T. Eddy, Ramesh Ramachandran  and Robert G. Griffin

      Version of Record online: 29 JUN 2009 | DOI: 10.1002/cphc.200900102

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      Targeting the hydrophobic core: Solid-state NMR rotational resonance width experiments are performed to measure 13C–13C distances between aromatic and aliphatic residues that make up the hydrophobic core of streptococcal protein G (see picture). Their value in structure calculations and the effect of chemical shift anisotropy at high magnetic field are discussed.

    24. Chemically Induced Unfolding of Bovine Serum Albumin by Urea and Sodium Dodecyl Sulfate: A Spectral Study with the Polarity-Sensitive Charge-Transfer Fluorescent Probe (E)-3-(4-Methylaminophenyl)acrylic Acid Methyl Ester (pages 1664–1671)

      Shalini Ghosh and Nikhil Guchhait

      Version of Record online: 22 MAY 2009 | DOI: 10.1002/cphc.200900161

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      Charge-transfer probe (E)-3-(4-methylaminophenyl)acrylic acid methyl ester (MAPAME) exhibits a blue shift and enhanced intensity of its charge-transfer emission band on binding to bovine serum albumin (BSA; see picture). These spectral changes can be used to investigate the MAPAME–BSA binding interaction and to monitor the unfolding of BSA induced by denaturants, such as urea and surfactant micelles.

    25. Force Spectroscopy of the Interaction Between Mycobacterial Adhesins and Heparan Sulphate Proteoglycan Receptors (pages 1672–1675)

      Vincent Dupres, Claire Verbelen, Dominique Raze, Frank Lafont and Yves F. Dufrêne

      Version of Record online: 27 MAY 2009 | DOI: 10.1002/cphc.200900208

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      New avenues in pathogenesis research: Single-molecule measurements using AFM elucidate the specific binding forces between pathogen–host interactions. A bacterial adhesin (HBHA) on the AFM tip detects single HSPG receptors directly on living host cells (see figure). In vivo HBHA-HSPG binding forces are similar to those measured in vitro for HBHA-heparin complexes.

  9. Conference Reports

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    1. From Single-Biomolecule Electrochemistry to Biosensors and Biofuel Cells (pages 1677–1679)

      Ernesto Julio Calvo

      Version of Record online: 26 MAY 2009 | DOI: 10.1002/cphc.200900252

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      The bioelectrochemistry symposium at the 59th annual meeting of the International Society of Electrochemistry (ISE) covered significant developments in this area—from biomimetics, redox proteins, and enzymes, to biosensors and biofuel-cell applications. This conference report highlights some of the most important contributions (the picture shows a schematic representation of an amperometric enzyme electrode, courtesy of P.N. Bartlett).

    2. Microscopic and Spectroscopic Observations in the Bio-Nanoworld (pages 1680–1682)

      Peter Hinterdorfer, Peter Pohl and Gerhard Schütz

      Version of Record online: 29 JUN 2009 | DOI: 10.1002/cphc.200900358

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      Biophysics in Linz: In February biophysicists from across the world converged on Linz for two biophysical conferences. The city which is the Cultural Capital of Europe 2009, provided the perfect environment for fruitful discussions on single-molecule techniques in biophysics, bio-nanotechnology, cell biology, and drug discovery.

  10. Preview

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Reviews
    7. Minireviews
    8. Communications
    9. Articles
    10. Conference Reports
    11. Preview
    1. You have free access to this content
      Preview: ChemPhysChem 11/2009 (page 1687)

      Version of Record online: 29 JUN 2009 | DOI: 10.1002/cphc.200990038

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