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Symposium Life Sciences on the Nanometer Scale - Physics Meets Biology Mittwoch Fachsitzungen – Haupt-, Kurzvorträge und Posterbeiträge – SYLS 1 Symposium ”Life Sciences on the Nanometer Scale - Physics Meets Biology” Zeit: Mittwoch 14:00–15:00 Raum: H 37 Hauptvortrag SYLS 1.1 Mi 14:00 H 37 Aquaporin Proteins: Perfect filters — •Helmut Grubmüller and Bert L. de Groot — Theoretische und computergestützte Biophysik MPI für biophysikalische Chemie, 37075 Göttingen Aquaporins are highly selective water channels. Molecular dynamics simulations of water permeation correctly predict the permeation rate, explain why these channels are so efficient, and suggest that protons are blocked by an electrostatic barrier. Hauptvortrag SYLS 1.2 Mi 14:30 H 37 Single-Molecule Cellular Signaling — •Thomas Schmidt — Physics of Life Processes, Leiden Institute of Physics, Leiden University Recent studies showed that several types of membrane microdomains are involved in H-Ras signal transduction. However, our knowledge about the in vivo dynamics of these domains is still in its infancy. In this study, the effect of plasma membrane organization on the activation of the small GTPase H-Ras was studied by single-molecule fluorescence microscopy. Diffusion analysis revealed a major, fast diffusing population and a minor, slow diffusion population for both inactive and active H-Ras. Activation of H-Ras resulted in a transfer from free diffusion to confinement into 200 nm-sized domains for the minor, slowly diffusing fraction. This is a first indication for the relevance of membrane ultrastructure on cellular signalling. SYLS 2 Symposium ”Life Sciences on the Nanometer Scale - Physics Meets Biology” Zeit: Mittwoch 15:15–16:00 Raum: H 37 SYLS 2.1 Mi 15:15 H 37 Nucleo-Cytoplasmic Transport of Single Molecules — •Ulrich Kubitscheck, Andreas Hoekstra, David Grünwald, Jan Peter Siebrasse, and Reiner Peters — Institute of Medical Physics and Biophysics, Westfälische Wilhelms-Universität, D-48149 Münster Understanding the intracellular exchange of matter and information across the envelopes of cell nuclei presents a central biophysical problem. Single-molecule microscopy was used to examine the topography and transport properties of the large pore complexes (NPCs) in the nuclear envelopes of digitonin-permeabilized cells. The nucleoporins POM121, Nup358 and Nup153 could be localized along the NPC axis with a precision of ±25 nm. Binding sites of NTF2 were detected on cytoplasmic filaments and in the central framework of the NPC. Binding sites of an import complex containing karyopherin β, however, were localized to the central framework, and extended up to 200 nm into the nuclear basket. In order to monitor the interaction of the transport substrates with the NPC in real-time, we used an electron-multiplying CCD for fast kinetic measurements. The dwell times of NTF2 and import complex at their NPC binding sites were determined as 8.2±0.4 and 16±0.6 ms, respectively. Together with the known transport rates these data suggest that nucleocytoplasmic transport occurs via multiple parallel pathways within single NPCs. SYLS 2.2 Mi 15:30 H 37 Biophysical Applications of Quantum Dots: Labeling of Single Biomolecules — •Colin D. Heyes 1 , Andrei Yu. Kobitski 1 , Elza V. Amirgoulova 1 , Vladimir V. Breus 1 , Kirill V. Anikin 1 , and G. Ulrich Nienhaus 1,2 — 1 Department of Biophysics, University of Ulm, D - 89069 Ulm, Germany — 2 Department of Physics, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA Fluorescent quantum dots (QDs) have several important properties, which render them extremely useful in ultrasensitive studies of biomolecular dynamics. They are bright, easily tunable in emission color, can be chemically modified at the surface to recognize specific biomolecules without changing the color, and are extremely stable against photobleaching. We have studied the single particle photophysics, such as fluorescence blinking and brightness, under various conditions to evaluate their usefulness in single biomolecular experiments. We then present examples in which they can be used to evaluate ultrasensitive and long timescale biophysical processes as well as, or better than, conventional fluorescent dyes. In the first example, we have studied the lateral diffusion of labeled lipid molecules. This allows us to track lipid molecules for long periods of time without significantly affecting the diffusion kinetics, as has been observed with latex bead tracking. In the second example, we have studied enzyme-substrate interactions of single enzyme molecules. Both examples highlight the fact that QDs will continue to increase in importance for biophysical applications, and the photophysics of such species needs to be thoroughly understood. SYLS 2.3 Mi 15:45 H 37 Detection and spectroscopy of 5 nm gold particles using white-light confocal microscopy — •Patrick Stoller 1 , Klas Lindfors 2 , Thomas Kalkbrenner 3 , and Vahid Sandoghdar 1 — 1 Physical Chemistry Laboratory; Swiss Federal Institute of Technology (ETH); CH-8093, Zurich; Switzerland — 2 Department of Physics; Helsinki University of Technology; P. O. Box 1000; FIN-02015 HUT; Finland — 3 FOM Institute for Atomic and Molecular Physics (AMOLF); Kruislaan 407; 1098 SJ Amsterdam; The Netherlands The interaction of fluorescently labeled biological molecules can be observed dynamically using optical microscopy. Gold nanoparticles can also be used to optically label biological molecules because of their welldefined plasmon resonance spectrum. Gold nanoparticles are biocompatible and, unlike fluorophores, they do not bleach. To avoid interference with the molecular interaction, it is important to minimize the size of the labels. Recently, Boyer et. al. succeeded in detecting 2.5 nm gold nanoparticles using photothermal imaging [Science. 297. 1160-1163]. In our work, we used white light confocal microscopy not only to detect but also to observe the plasmon resonance spectrum of single gold nanoparticles with diameters as small as 5 nm [submitted]. An ultra-short pulse laser and a photonic crystal fiber were used to generate a collimated beam of quasi-continuum white light, which was tightly focused onto the sample using a high numerical aperture microscope objective; the scattered light was collected confocally and detected using an imaging spectrometer. Our goal is to apply this technique to studying the interaction of biological molecules at the single molecule level.
Symposium Life Sciences on the Nanometer Scale - Physics Meets Biology Mittwoch SYLS 3 Symposium ”Life Sciences on the Nanometer Scale - Physics Meets Biology” Zeit: Mittwoch 16:00–18:30 Raum: B SYLS 3.1 Mi 16:00 B Accumulation and Replication of DNA driven by temperature gradients — •Dieter Braun — Emmy Noether Gruppe, Experimentalphysik, Universitaet Muenchen, Amalienstr. 54, 80799 Muenchen The influence of temperature gradients on DNA is investigated. For the first time, the thermophoresis of DNA from hot to cold was measured. Under conditions which also allow for convection, thermophoresis accumulates DNA thousandfold into microscopic pots [1]. R. Piazza showed that thermophoresis of ions such as DNA in water is probably driven and dominated by a gradient of interfacial tension at the nanoscopic interface between molecule and water [2]. In a similar geometry, the laminar convection can be used to drive the DNA amplifying reaction of PCR. Such a laminar convective PCR amplifies DNA specifically and quantitatively at a speed faster than standard PCR machines [3]. Both studies of mesoscopic open system far away from thermodynamic equilibrium revealed new effects. Besides biotechnological applications, the experiments suggests a convective origin of life in porous rock near submarine hydrothermal vents [4]. [1] D. Braun and A. Libchaber, PRL 89:188103 (2002) [2] R. Piazza and A. Guarino, PRL 88:208302 (2002) [3] D. Braun, N.L. Goddard and A. Libchaber, PRL 91:158103 (2003) [4] D. Braun and A. Libchaber, Physical Biology, submitted SYLS 3.2 Mi 16:00 B Modulation of the Nanoscale-Structure of Fibronectin Fibrils — •Tilo Pompe — Institut für Polymerforschung Dresden e.V. & Max- Bergmann-Zentrum für Biomaterialien Dresden The protein fibronectin is a major component of the extracellular matrix providing cells with binding sites to the surrounding tissue. The formation of fibrils from single fibronectin molecules is a complex process which includes binding of cell receptors, like integrins, conformational changes of fibronectin by mechanical forces exerted from the cell, and polymerisation of fibronectin molecules at newly exposed binding sites. Scanning force microscopy analysis revealed that early stages of fibronectin fibrillogenesis are controlled by the binding strength of fibronectin molecules to the underlying polymer substrate. Furthermore, the nano-structure of the fibrils exhibits characteristic distances between small fibrils with a distinct periodicity of 73 nm. The periodic spacing implies a mechanism of the fibrillogenesis process directly related to the force applied to the protein via the cytoskeleton of the cell. SYLS 3.3 Mi 16:00 B Interactions of Thionin with DNA-Strands: Intercalation vs External Stacking — •Christoph Hecht 1 , Josef Friedrich 1 , and Ta-Chau Chang 2 — 1 TU München, Physik-Department E14, Lehrstuhl für Physik Weihenstephan, 85350 Freising — 2 Institute of Atomic and Molecular Science, Academia Sinica, Taiwan The interaction of dye-molecules with DNA-strands plays an important role in anti-cancer drug research. We investigated the binding modes of thionin with various structures of short stranded DNA-molecules by measuring the response of a spectral hole to pressure variations. Thionin binds through Coulomb-interaction via external stacking to DNA-quadruplex structures. The binding to DNA-duplex structures, however, is different: One of the two possible isomers of thionin intercalates into the DNAstrands. SYLS 3.4 Mi 16:00 B SINGLE VIRUS TRACING: VISUALIZATION OF THE IN- FECTION PATHWAY OF A VIRUS INTO A LIVING CELL — •T. Endreß, S. Mugrauer, A. Zumbusch, and C. Bräuchle — Department Chemie, Universität München, Butenandtstr. 11, 81377 München, Germany Viruses play a major role in biology and medicine. A detailed analysis of the different steps of a viral infection is not only necessary to understand viral biology, but also for the development of efficient antiviral drugs and save viral gene therapy vectors. Single Virus Tracing allows visualization of the infection pathway of an individual virus labeled with fluorescent dye molecules (even in the case of labeling with a single dye molecule). The fluorescence of the marker molecule is imaged and used to follow the pathway of the virus with high spatial (≥ 40 nm) and time (≥ 10 ms) resolution. As a first model system we have investigated the infection pathway of Adeno-associated viruses (AAV) into HeLa cells. AAV shows promising results for the use in gene therapy applications. A sequence of events can be tracked starting with a virus approaching the cell surface, successive receptor binding, membrane penetration, endosome formation and trafficking, virus release from the endosome and virus trafficking in the cytoplasm as well as penetration into the nuclear area. Besides AAV the studies have been extended to other viral particles like HIV. HIV is an enveloped virus, which was labeled at its matrix protein (MA) and its viral protein (Vpr) with GFP and GFP mutants. First results from these studies will also be presented. SYLS 3.5 Mi 16:00 B Interactions of biopolymers of fixed topology with thermal fluctuations — •Ralf Metzler 1 and Andreas Hanke 2 — 1 NORDITA, Blegdamsvej 17, DK-2100 Copenhagen OE — 2 Theoretical Physics, University of Oxford, Oxford OX1 3NP, United Kingdom DNA knots of different complexity effect different mobility of the chain, and they pose an intricate problem to a biological cell in respect to transcription or replication. Specific enzymes remove knots very efficiently despite having access to local information, only. I will discuss ideas on how interaction of thermal fluctuations with the fixed topology of the chain may assist the enzymes in their task, and under which conditions this may actually work in vivo. Double-stranded DNA even at physiological temperatures undergoes fluctuations, during which single-stranded bubbles open up along the strand. Increasing the temperature, dsDNA eventually undergoes a melting transition. Starting from a microscopic model for the Free energy, we derive a Fokker-Planck equation to the bubble fluctuations, whose predictions close to physiological temperatures reproduce recent experimental results on single bubble fluctuations. References: R. Metzler, A. Hanke, P. G. Dommersnes, Y. Kantor, and M. Kardar, Phys. Rev. Lett. 88 (2002) 188101; Phys. Rev. E 65 (2002) 061103. A. Hanke and R. Metzler, Phys. Rev. Lett. 90 (2003) 159801, A. Hanke and R. Metzler, J. Phys. A (Lett.) 36 (2003) L473. SYLS 3.6 Mi 16:00 B Tuning of microcapsule adhesion by varying capsule stiffness — •Nils Elsner and Andreas Fery — MPI for Colloids and Interfaces 14424 Potsdam We have been studying the adhesion polyelectrolyte (PE) capsules composed from Polyallylamine (PAH) and Polystyrenesulfonate (PSS). These PE capsule can be produced in sizes up to 20 mm, while the thickness remains tunable on the nanometer scale. This makes it possible to vary the elastic properties by changing the wall thickness, which has been shown by us recently [1]. The interaction of these capsules with a glass surface was studied by Reflective Interference Contrast Microscopy measurements. It was found, that negatively charged capsules adhere to glass, which was coated with positively charged polyelectrolyte, whereas these capsules do not adhere to bare glass. We found that the adhesion area increases with decreasing shell thickness for shells with identical surface interactions. The data for the adhesion area for different thicknesses and different radii could be fitted with a simple model based on [2], having the surface energy as the only fitting parameter. In pH-experiments, the stiffness of the capsules is found to decrease upon increasing pH as revealed by force spectroscopy measurements. Consequently, we observe an increase of the adhesion areas although the surface interactions are not strongly changed in this pH range. [1] F. Dubreil, N. Elsner, and A. Fery, Eur. Phys. J. E in press (2003). [2] L. D. Landau and E. M. Lifschitz, Elastizitätstheorie (Akademie Verlag, Berlin, 1991). SYLS 3.7 Mi 16:00 B Persistent Spectral Labeling of Proteins via UV- Photochemistry of their Aromatic Amino Acids — •Christoph Schnell, Christoph Hecht, Markus Stübner, and Josef Friedrich — Physik-Department E14, Lehrstuhl für Physik Weihenstephan, Technische Universität Müenchen, 85350 Freising We used hole burning techniques for high resolution frequency label-
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