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Plenarvorträge - DPG-Tagungen

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Symposium Life Sciences on the Nanometer Scale - Physics Meets Biology Mittwoch<br />

optical properties of the whole complex.<br />

SYLS 3.22 Mi 16:00 B<br />

Ab-initio vibrational analysis of the secondary structure of proteins<br />

— •Lars Ismer 1 , Joel Ireta 1 und Jörg Neugebauer 2 —<br />

1 FHI Berlin — 2 Universität Paderborn<br />

For a detailed understanding of protein functionality an accurate description<br />

of their dynamical properties is crucial. However, so far ab-initio<br />

based studies on realistic structures going beyond the primary structure<br />

are rare, particularly with respect to vibrational properties. We have therefore<br />

performed a full ab-initio DFT-PBE based harmonic vibrational<br />

analysis of infinite poly-alanine and -glycine chains in two different secondary<br />

conformations: the infinite α-helical conformation, as model for the<br />

most ubiquitous native secondary conformation stabilized by hydrogen<br />

bonds (hb) and the fully extended conformation (FES), as a reference<br />

system where hb’s are absent. By comparing the phonon dispersion relation<br />

of α-helix and FES we were able to extract a direct ”fingerprint”<br />

of the hb’s and their cooperativity in specific high frequent vibrational<br />

branches. We also observed that constraining the peptide chain to the<br />

helical conformation leads to significant blue-shifts in the low frequent<br />

backbone vibrations. A thermodynamic analysis based on these results<br />

revealed that the vibrational contributions of the free energy significantly<br />

lower the stability of the α-helix with respect to the FES by about 0.8<br />

kcal/mol at 300K.<br />

SYLS 3.23 Mi 16:00 B<br />

Optical characterisation of artifical confinements for protein<br />

folding — •Johannes Hohlbein 1 , Ulrike Rehn 1 , and Ralf B.<br />

Wehrspohn 2 — 1 Max-Planck-Institute of Microstructure Physics,<br />

Weinberg 2, 06120 Halle, Germany — 2 Department of Physics,<br />

University of Paderborn, Warburger Str. 100, 33098 Paderborn,<br />

Germany<br />

We present a new method to characterize in-situ the optical thickness<br />

of porous alumina films by the use of photoluminescence-induced Fabry-<br />

Pèrot-interferences. Additionally we show, that the use of different electrolytes<br />

yields different photoluminescence pattern. A second experiment<br />

allows to determine the degree of filling of the pores by a liquid which is<br />

of importance when using the pores as templates for protein folding. First<br />

studies of the influence of geometrical confinement on protein folding will<br />

be presented.<br />

Porous oxide growth on aluminium under anodic bias in various electrolytes<br />

has been studied for nearly 50 years. Recently, porous anodic<br />

alumina (PAA) films have been used to prepare nanostructures for a<br />

wide range of applications. In order to use porous alumina as template<br />

for protein folding in-situ optical measurements of their thickness as well<br />

as the degree of filling are required. It has been shown, that porous alumina<br />

exhibits a photoluminescence (PL) signal. We will use the PL pattern<br />

to determine the thickness and the degree of filling by Fabry-Pèrotinterferences.<br />

SYLS 3.24 Mi 16:00 B<br />

Neuronale Synchronität in biologisch plausiblen exzitatorischen<br />

Netzwerken: Entstehung und Modulation — •K. Kube 1 , V.<br />

Spravedlyvyy 1 , A. Herzog 1 , B. Michaelis 1 , A. de Lima 2 , T.<br />

Opitz 2 , T. Voigt 2 , A. Reiher 3 , A. Krtschil 3 , S. Günther 3 , H.<br />

Witte 3 und A. Krost 3 — 1 Institut für Elektronik, Signalverarbeitung<br />

und Kommunikationstechnik, Otto-von-Guericke-Universität Magdeburg<br />

— 2 Institut für Physiologie, Otto-von-Guericke-Universität Magdeburg<br />

— 3 Institut für Experimentelle Physik, Otto-von-Guericke-Universität<br />

Magdeburg<br />

Detaillierte Kompartimentmodelle von Einzelneuronen sind oft benutzt<br />

worden, um das Gehirn als modulare elektrische Apparatur darzustellen.<br />

Wir präsentieren eine biologisch realistische Simulation von<br />

Netzwerk-Eigendynamik, wie sie in Zellkulturen des frühen zerebralen<br />

Kortex von Wirbeltieren abläuft. Dabei wird die Entwicklung der<br />

natürlichen Vernetzungstruktur nachgebildet, in der verschiedene funktionelle<br />

Neuronentypen interagieren. Ausgehend von spontaner elektrischer<br />

Aktivität einzelner Neurone werden in massiven Simulationen Eigenarten<br />

der elektrischen Dynamik des Netzwerks und deren gezielte<br />

Beeinflussung gezeigt sowie mit der in-vitro-gemessenen Aktivität verglichen,<br />

die in Verbindung mit zellulären Lernmechanismen (Hebb-LTP)<br />

wechselwirken können, um sich an Muster äußerer Reize anzupassen. Abschließend<br />

wird diskutiert, auf welche Art man in spontan feuernden Zellen,<br />

die über zufällige, rekurrente Strukturen von Netzwerken verbunden<br />

werden, von Organisation sprechen kann.<br />

SYLS 3.25 Mi 16:00 B<br />

Protein adsorption on tailored substrates — •Hubert Mantz,<br />

Anthony W. Quinn, and Karin Jacobs — Experimental Physics,<br />

Saarland University, POB 151 150, 66041 Saarbrücken<br />

It has long been established that bacterial plaque plays an essential role<br />

in the development of oral diseases such as dental caries. Dental plaque<br />

consists of a diversity of different components, which makes it difficult to<br />

determine the mechanism for their formation and growth. Understanding<br />

them would enhance the field of preventative dentistry enabling restorative<br />

materials to be tailored to resist bacterial attachment or have some<br />

antibacterial effect.<br />

We try to get an insight in these mechanisms by using ellipsometry, a<br />

non-destructive optical method for determining film thickness and optical<br />

properties of the sample to be studied. These experiments can measure<br />

the adsorption kinetics of purified salivary proteins on tailored substrates.<br />

By using AFM and wettability analysis, the composition of the surfaces<br />

can be controlled and described.<br />

SYLS 3.26 Mi 16:00 B<br />

Picosecond dynamics of bacterial porins investigated by<br />

quasi-elastic neutron scattering — •Marie Plazanet 1 , Cecile<br />

Bon 2 , Franck Gabel 3 , Sylviane Julien 2 , Peter Timmins 1 ,<br />

and Guiseppe Zaccai 3 — 1 Institut Laue Langevin, 6 rue Jules<br />

Horowitz, 38042 Grenoble Cedex 9, France — 2 CNRS/IPBS, 205 route<br />

de Narbonnes, 31077 Toulouse cedex, France — 3 IBS, 41, rue Jules<br />

Horowitz, 38027 Grenoble Cedex 1, France<br />

The survival of bacteria requires a continuous exchange of molecules<br />

across the cell wall. Porins, a large class of membrane proteins, are involved<br />

in the transport of small hydrophilic molecules across the outer<br />

membrane. Porins have peculiar structural features; they fold in a multistranded,<br />

closed beta-sheet, exposed to the hydrophobic membrane core<br />

on one side and an aqueous channel on the other. Dynamics of these extremely<br />

stable proteins clearly modulate the pore activity (i.e. biological<br />

activity of the porin), and there is good evidence that this dynamics is<br />

modulated by the dynamics of the lipids surrounding the porins.<br />

Experiments have been undertaken on outer membrane fractions of<br />

E.Coli, with the natural asymmetric lipid distribution (lipopolysaccharides<br />

in the outer leaflet and various phospholipids in the inner leaflet).<br />

Samples enriched in porins and samples depleted in porins have been investigated<br />

to probe both lipid and porin contribution. While data are still<br />

under study, preliminary results show that both systems clearly exhibit<br />

very different dynamics on the pico-second timescale. A brief comparison<br />

with corresponding results on the bacteriorhodospsin, a representative of<br />

the membrane proteins folded in an helix-bundle, will be done.<br />

SYLS 3.27 Mi 16:00 B<br />

Controlled proliferation of living cells on UV-light modified polymers<br />

— •Thomas Gumpenberger 1 , Johannes Heitz 1 , Dieter<br />

Baeuerle 1 und Christoph Romanin 2 — 1 Angewandte Physik, Universitaet<br />

Linz, Austria — 2 Biophysik, Universitaet Linz, Austria<br />

We demonstrated the controlled proliferation of human umbilical endothelial<br />

cells (HUVEC) on UV-light modified polymer samples. The polymers<br />

under investigation were either polytetrafluoroethylene (PTFE)<br />

or polyethyleneterephtalate (PET), which are among the most frequently<br />

employed biomaterials in reconstructive medicine. The PTFE surfaces<br />

were modified by exposure to the ultraviolet (UV) light of a Xe2*-excimer<br />

lamp at a wavelength of 172 nm in an ammonia atmosphere. The irradiation<br />

led to an efficient exchange of the F-atoms in the surface by other<br />

chemical moieties. In-vitro, this resulted in a significant increase in the<br />

number of adhering cells 1 day after seeding and in the formation of a<br />

confluent cell layer after 3 to 8 days. The results were comparable or even<br />

better than those obtained on standard polystyrene petri-dishes used in<br />

cell cultivation. Similar studies were performed on PET.<br />

SYLS 3.28 Mi 16:00 B<br />

Electrolytic fabrication of SNOM aperture-sensors — •Carola<br />

Haumann, Christoph Pelargus, Robert Ros, and Dario Anselmetti<br />

— Experimental Biophysics and Applied Nanosciences, Faculty<br />

of Physics, Bielefeld University, Universitaetsstrasse 25, 33615 Bielefeld,<br />

Germany<br />

The resolution achievable with scanning near-field optical microscopy<br />

(SNOM) is determined by the optical quality of the near-field sensors.<br />

We present a method to fabricate reproducibly aperture probes with diameters<br />

in the sub 100nm range by solid state electrolysis. The method,<br />

originally invented by A. Bouhelier et al., was further developed by in-

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