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Symposium Life Sciences on the Nanometer Scale - Physics Meets Biology Donnerstag of loading rate-dependent behaviour were identified. A thermal off-rate koff = (1.2 ± 1.0) × 10 −3 s −1 was derived from the lower loading rate regime for all DNA fragments. In the upper loading rate regime, however, these fragments exhibited distinct differences which are attributed to sequence specific details of the binding mechanism. SYLS 4.3 Do 10:15 H 37 Fast Folding Dynamics of α-Helical Peptides — •Martin Volk, Angela Pozo Ramajo, Edmund Leary, and Sarah A. Petty — Department of Chemistry, University of Liverpool, UK The dynamics of secondary structure formation, which is generally believed to be the first phase of protein folding, has attracted much attention recently, particularly since the application of the temperature jump technique. Using nanosecond lasers, a sudden temperature increase is induced; the ensuing (un)folding can then be observed by suitable timeresolved methods, such as IR-spectroscopy. Previous studies on α-helical model peptides investigated alanine-based peptides containing a repeat motif of the type -(AAAXA)n- (X: hydrophilic amino acid, n = 2-4), which show helix-coil relaxation on the time scale of 150-300 ns. Here, we report results on longer and more complex helical peptides. We found that the helix-coil relaxation in Poly-N 5 -(3-hydroxypropyl)-Lglutamine (DP 230) occurs on the same time scale as in alanine-based peptides, in spite of the peptide length and the complex and bulky side chain. On the other hand, the helix-coil relaxation in the random copolymer Poly(Ala, Lys, Glu, Tyr) 6:5:2:1 (DP 180) is much more complex. At high concentrations, it occurs on the µs-time scale and seems to be limited by strong interpeptide interactions of the abundant charged residues, whereas at lower concentrations it shows major deviations from monoexponentiality due to sequence heterogeneity. SYLS 4.4 Do 10:30 H 37 Photomodulation of conformational states — •Christian Renner, Alexander Milbradt, Markus Schütt, Raymond Behrend, Simone Krupka, Eva-Karthin Sinner, Ciara Cabrele, and Luis Moroder — Max-Planck-Institut für Biochemie Every living cell, be it bacterial or human, contains a variety of proteins that turn the static information encoded in the genes into the densely packed activity of life. Although protein functions are built on well-known fundamental physical laws the sheer complexity of such macromolecules due to their size and variability renders experimental as well as theoretical investigations a difficult challenge. A productive and helpful approach has been the reduction to simpler albeit artificial model systems. We have constructed peptide models that combine small functional protein fragments of a few amino acid residues with a light-switch allowing for photomodulation of properties like spatial structure, redox potential or affinity for ligands. The light induced changes could be exploited for a limited photo-control of peptide structure (1), protein binding (2) and oxidative protein refolding (3). The consequences observed upon applying well-defined changes to the system through the photoisomerization process should allow for a better understanding of the functional protein parts that are contained in our model systems. (1) Biopolymers 63 (2002), 382-393.; (2) Angew. Chem. Int. Ed. 41 (2002), 289-292.; (3) Chem. Biol. 10, 487-490. SYLS 4.5 Do 10:45 H 37 Electro-Manipulation of Oligonucleotides Tethered to Au- Surfaces — •Ulrich Rant 1 , Kenji Arinaga 1,2 , Shozo Fujita 2 , Naoki Yokoyama 2 , Gerhard Abstreiter 1 , and Marc Tornow 1 — 1 Walter Schottky Institut, Technische Universitaet Muenchen, 85748 Garching, Germany — 2 Fujitsu Laboratories Ltd., 10-1 Morinosato-Wakamiya, Atsugi 243-0197, Japan We present electro-optical investigations of short DNA strands, tethered to Au-electrodes in aqueous solutions. By controlling the bias potential at the supporting electrodes, we are able to study multiple phenomena related to electrostatic interactions between polyelectrolytes and metal interfaces in electrolyte environment: DNA-desorption at highly negative electrode potentials can be utilized to study the electrostatic nature of DNA, revealing a new regime of excessive counterion condensation in solutions of high salt concentrations. In contrast, by employing moderate AC-potentials with respect to the potential of zero charge, we are able to attain persistent conformational switching with formidable long term stability of the DNA layer on the Au- surface, alternating the orientation of the strands between a lying‘ and a ’ ’ standing‘ state. We elucidate the capability of the presented modulation experiments to provide information on collective monolayer properties such as steric interactions between adsorbed molecules, as well as the possibilities to study molecular dynamics of tethered DNA subjected to electric fields at the metal/solution interface. SYLS 5 Symposium ”Life Sciences on the Nanometer Scale - Physics Meets Biology” Zeit: Donnerstag 11:15–12:30 Raum: H 37 Hauptvortrag SYLS 5.1 Do 11:15 H 37 Mechano-Chemical Coupling in F1-ATPase — •Kazuhiko Kinosita — Center for Integrative Bioscience, Okazaki National Research Institutes The protein F1-ATPase is a rotary motor made of a single molecule. Its central γ subunit rotates against a surrounding cylinder made of α3β3 subunits. This rotary motor is powered by sequential ATP hydrolysis in the three β subunits, and reverse rotation of the motor is expected to drive ATP synthesis. We have shown, by single-molecule imaging, that (i) the rotary torque is nearly independent of the rotation angle, (ii) 80- 90 pN nm of mechanical work can be done per ATP hydrolyzed, (iii) binding of ATP causes ∼90 o rotation, and (iv) release of the last hydrolysis product causes further ∼30 o rotation. Point ii implies that the efficiency of chemo-mechanical conversion may reach ∼100 %. Points i-iv allowed us to infer the angle-dependent potential energies for γ rotation for each of chemical intermediates that appear during rotation. Details of the coupling scheme between chemical reactions on the three catalytic sites and mechanical rotation of the rotor are beginning to unravel. SYLS 5.2 Do 11:45 H 37 Probing individual F0F1 ATP synthases by multi-parameter fluorescence spectroscopy — •Michael Prummer 1 , Horst Vogel 1 , Beate Sick 2 , Alois Renn 3 , Gert Zumofen 3 , Urs P. Wild 3 , Georg Kaim 4 und Peter Dimroth 4 — 1 Institute of Biomolecular Sciences, EPFL, CH-1015 Lausanne — 2 DNA-Array Facility, University of Lausanne, CH-1015 Lausanne — 3 Physical Chemistry Laboratory, ETH-Hönggerberg, CH-8093 Zürich — 4 Institute of Microbiology, ETH- Zentrum, CH-8092 Zürich The rotary motor F0F1 ATP synthase is the universal ATP factory in most cells from bacteria to plants and animals. The driving force for ATP production is a trans-membrane potential plus a H + /Na + gradient. Vice versa, F0F1 can act as an ion pump by consuming ATP and is thus a completely reversible rotor. We have simultaneously measured several fluorescence quantities from individual immobilized and functionally coupled F0F1 rotary motors by single-fluorophore multi-parameter confocal microscopy. By analyzing these quantities we could monitor the rotation of F0F1 during ATP synthesis and hydrolysis. We could further correlate for example the different distributions of the fluorescence lifetime or the emission spectral ratio with structural and functional features of the protein. SYLS 5.3 Do 12:00 H 37 Molecular dynamics simulations of isolated β-subunits of F1- ATPase — •U. Kleinekathöfer 1 , B. Isralewitz 2 , M. Dittrich 2 , and K. Schulten 2 — 1 International University Bremen, 28725 Bremen — 2 Beckman Institute, University of Illinois, Urbana-Champaign, USA. The F1 unit of ATPase has three-fold symmetry and consists of three noncatalytic α and three catalytic β-subunits. The β-subunits furnish the binding sites where ADP is transformed into ATP. We have investigated the properties of isolated β-subunits as a step towards explaining the function of the integral F1 unit. The β-subunits exist in different conformations at any moment of the F1 unit reaction cycle. The open conformation of the AlF3-inhibited β-subunit of bovine ATPase had been equilibrated for about 10 ns and a spontaneous change in conformation was observed. The change can be decomposed into two rotations: one around an axis parallel to the pseudo-symmetry axis of F1- ATPase and one around an axis perpendicular to the first axis . In several runs the equilibrated subunit was in a conformation about half-way between the open and the closed conformation. This partially confirms the
Symposium Life Sciences on the Nanometer Scale - Physics Meets Biology Donnerstag assumption that elastic energy is stored in the open confirmation. It is unclear if there is a further spontaneous closing motion on longer time scales. To test the effect of the adjacent alpha subunit we performed simulations of the joined units and found only a negligible effect. We also equilibrated isolated β-subunits for the AlF − 4 -inhibited F1-ATPase starting from the the half-closed state with ADP bound and from modified half-closed states with bound ATP. The simulations again revealed spontaneous motion towards the closed conformation. SYLS 5.4 Do 12:15 H 37 A molecular machine based on a DNA aptamer — •Friedrich Simmel, Wendy Huynh, and Andreas Reuter — Sektion Physik and Center for Nanoscience, LMU Muenchen, Geschwister-Scholl-Platz 1, 80539 Muenchen A functional nanomechanical DNA switch based on the anti-thrombin aptamer structure is presented. Utilizing DNA strand displacement by branch migration, thrombin can be selectively bound or released by the DNA machine. The operation of the machine is demonstrated by electrophoretic mobility shift assays and fluorescence resonance energy transfer experiments.
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Ausschuss Industrie und Wirtschaft
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Page 519 and 520: A. D., Mirlin .................HL 1
Page 521 and 522: Breidenbach, Boris ........ AKB 50.
Page 523 and 524: Elli, Alexandra .............SYLS 3
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Martin, Tobias ............. MA 13.
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Partyka, Ewa ................ M 18.
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Rugeramigabo, Eddy Patrick O 14.38,
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Sihler, J. .................... DS
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Volz, K. .................... HL 44
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