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Plenarvorträge - DPG-Tagungen

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Arbeitskreis Biologische Physik Freitag<br />

crease, which may occur either by releasing intra-molecular voids or by<br />

contraction of the solvent near the newly exposed protein surface. The<br />

latter involves changes in structure of the protein-solvent network. By<br />

dynamic neutron scattering we probe the pressure evolution of proteinsolvent<br />

bonds. At the unfolding transition, we observe a reduction of the<br />

structural inter-conversion rates and of water fluctuational amplitudes,<br />

related to a compressibility change. This result suggests that stronger<br />

protein-solvent interactions in the unfolded form destabilize the native<br />

state at high pressure. Neutron diffraction experiments reveal a reorganisation<br />

in the hydration shell upon unfolding in parallel with a decrease in<br />

helix content. About 40 intact in the pressure-unfolded state indicative<br />

of a molten globular conformation.<br />

AKB 50.62 Fr 10:30 B<br />

Collective dynamics of lipid membranes studied by inelastic<br />

neutron scattering — •Maikel C. Rheinstädter 1,2 , Christoph<br />

Ollinger 3 , Giovanna Fragneto 1 , and Tim Salditt 3 — 1 Institut<br />

Laue-Langevin, 6 rue Jules Horowitz, 38042 Grenoble, France — 2 IFF,<br />

FZ-Jülich, 52425 Jülich, Germany — 3 Institut für Röntgenphysik, Georg-<br />

August-Universität Göttingen, Geiststr. 11, 37073 Göttingen, Germany<br />

The collective dynamics of lipid molecules are believed to affect significantly<br />

the physical properties of phospholipid membranes. In the context<br />

of more complex biological membranes, collective molecular motions may<br />

play a significant role for different biological functions [1]. We present a<br />

first time inelastic neutron scattering study on the collective dynamics of<br />

the lipid acyl chains in the model system DMPC -d54. We have measured<br />

the dynamical structure factor S(Qr, ω) in the gel (Lβ) and the fluid (Lα)<br />

phase of the lipid bilayer. The dispersion relation we find is similar to<br />

those found in liquids, with a distinct minimum at Q0, the maximum of<br />

the static structure factor S(Qr), and can be compared to recent Molecular<br />

Dynamics simulations [2]. Furthermore, we investigated the temperature<br />

dependence of the excitations in the minimum in the vicinity of<br />

the main phase transition. Our discussion may shed light on the gel-fluid<br />

phase transition and coexistence of the two phases. By combining neutron<br />

diffraction and inelastic measurements, we gain information about<br />

structure and (collective) dynamics of model membranes on a molecular<br />

length scale. [1] R. Lipowsky and E. Sackmann, Handbook of Biological<br />

Physics, vol. 1, Elsevier (1995); [2] M. Tarek et al., Phys. Rev. Lett. 87,<br />

238101 (2001).<br />

AKB 50.63 Fr 10:30 B<br />

Investigation of the N-terminal domain of LHCII using single<br />

molecule techniques — •Felix Neugart 1 , Sebastian Schuler 1 ,<br />

Carsten Tietz 1 , Jörg Wrachtrup 1 , Stephanie Boggasch 2 , and<br />

Manuel Lion 2 — 1 3. Physikalisches Institut, Universität Stuttgart —<br />

2 Institut für Allgemeine Botanik, Universität Mainz<br />

The light-harvesting complex II (LHCII) is the most abundant<br />

chlorophyll-binding complex in photosynthesis of green plants. The<br />

native LHCII trimer is responsible for the absorption of half the photons<br />

involved in photosynthesis of algae and higher plants.<br />

The structure of the transmembrane part of the protein of the LHCII<br />

is well known (Kühlbrandt et al. 1994, Nature 367, 614-621) whereas the<br />

N-terminal region of the LHCII complex is not resolved and its function,<br />

orientation and dynamic is still under debate.<br />

One possibility to gather information about the motion of the Nterminal<br />

domain is to attach an artificial fluorophor to the N-terminus<br />

and observe the energy transfer to the Chlorophylls of the LHCII. Different<br />

conformations of the N-terminal domain lead to different energy<br />

transfer rates. Hence, the observation of single labeled LHCII-Monomers<br />

in a confocal setup monitors the dynamics of the N-terminal region and<br />

reveal subensembles of different conformations.<br />

AKB 50.64 Fr 10:30 B<br />

Continuum theory of filamental self-organization —<br />

•Alexander Zumdieck, Karsten Kruse, and Frank Jülicher<br />

— Max-Planck-Institut für Physik komplexer Systeme<br />

The cytoskeleton is a dynamic complex network of protein filaments<br />

which is involved in many active cellular processes. The polymerization<br />

and depolymerization of filaments as well as the interaction with other<br />

proteins such as molecular motors induce mechanical stresses and dynamic<br />

processes in these structures.Linear filament bundles are important<br />

substructures of the cytoskeleton.<br />

We discuss a general continuum description of the dynamics of such<br />

active networks[1] and focus on one-dimensional bundle geometries. We<br />

show that polymerization and depolymerization play a key role for the<br />

dynamic properties of a bundle, they for example introduce a new length<br />

scale in the system which governs instabilities leading to inhomogenous<br />

states. We relate this continuum theory to a more microscopic description<br />

of active filament systems and show that de-/polymerization could play<br />

a similar role as motors for bundle dynamics. The continuum description<br />

can also be applied to higher dimensional filament geometries that are<br />

for example relevant to the formation of filament rings on cell surfaces.<br />

[1] K. Kruse, A. Zumdieck and F. Jülicher, Europhys. Lett. 64, 716<br />

(2003)<br />

AKB 50.65 Fr 10:30 B<br />

Spontaneous Oscillations by hair bundles from the vertebrate<br />

inner ear — •Björn Nadrowski 1 , Pascal Martin 2 , and Frank<br />

Jülicher 1 — 1 Max-Planck-Institut für Physik komplexer Systeme,<br />

Nöthnitzer Straße 38, D-01187 Dresden, Germany — 2 Laboratoire<br />

Physico-Chimie Curie, Unité Mixte de Recherche 168, Institut Curie, 26<br />

rue d’Ulm, F-75248 Paris Cedex 05, France<br />

Hearing relies on active filtering to achieve exquisite sensitivity and<br />

sharp frequency selectivity. In a quiet environment, the ears of many<br />

vertebrates emit one to several tones. These spontaneous otoacoustic<br />

emissions, the most striking manifestation of the inner ear’s active process,<br />

must result from self-sustained mechanical oscillations of aural constituents.<br />

As early as 1948, Thomas Gold proposed that the ear contains<br />

an active amplifier, and predicted oto-acoustic emissions for malfunctioning,<br />

i.e. over-amplified ears. It has recently been shown that the<br />

mechanosensitive hair bundles of vestibular cells from the frog ear have<br />

the ability to oscillate spontaneously. This spontaneous oscillation leads<br />

to frequency-selective amplification and nonlinearity in the bundles mechanical<br />

response. We discuss the physical principles behind detection<br />

based on critical oscillation as well as specific mechanisms that can lead<br />

to oscillations and active behaviors by hair bundles. A simple theoretical<br />

description of the hair bundle is presented, and its implications are<br />

studied. The hair bundles non-linear response to mechanical stimuli is<br />

described. We pay special attention to the role of noise in the system.<br />

AKB 50.66 Fr 10:30 B<br />

Structure and Fluctuations of Highly Oriented and Charged<br />

Membranes Under Osmotic Stress. — •Guillaume Brotons, Ulrike<br />

Mennicke, and Tim Salditt — Institut fuer Roentgenphysik,<br />

Universitaet Goettingen<br />

Imposing osmotic pressure to multilamellar membranes is a unique<br />

method for studing lipid bilayer interactions [1]. We have extended this<br />

approach to charged lamellar phases oriented on flat solid support, which<br />

are then probed by interface sensitive X-ray scattering. In this first study<br />

we used the anionic phospholipid POPS [2] and synthetic cationic surfactant<br />

DDABr [3], at controlled osmotic stress corresponding to water<br />

layer thicknesses in the range of a few water molecules up to more than<br />

15 times the bilayer thickness. High-pressures (deshydrated) are obtained<br />

by controlled water vapour, while lower pressures (full hydration) are imposed<br />

by direct contact with a polyelectrolyte solution of same sign as<br />

the lamellar phase under investigation. Under these conditions, specular<br />

and non-specular reflectivity can be carried out within the different symmetry<br />

axes of the oriented membranes (Fig.1) which opens new routes<br />

for establishing the Equations Of State (Pressure-Distance diagram) of<br />

bio-molecular assemblies and studing bilayer undulations or compressibility<br />

fluctuations as a function of pressure. [1] Parsegian,V.A. et all,<br />

Methods in Enzymology; Academic-Press 1986; Vol.127. [2] Mennicke,U.,<br />

PhD-Dissertation, Göttingen-Universität, 08/2003. [3] Brotons,G. et all,<br />

Langmuir 2003, 19, 8235-8244.<br />

AKB 50.67 Fr 10:30 B<br />

X-ray and neutron reflectivity analysis of peptide-lipid model<br />

systems — •Chenghao Li und Tim Salditt — Institut fuer Roentgenphysik,<br />

Universitaet Goettingen<br />

Using x-ray and neutron reflectivity, we have investigated the structure<br />

of solid-supported, multilamellar lipid membranes with and without<br />

membrane active, antimicrobial peptides. To analyse the measured<br />

reflectivity curve we fit the curves to a model bilayer profile<br />

of adjustable resolution and deduce detailed structural parameters<br />

of the bilayers on an absolute scale of the scattering length<br />

density. The model is implemented in the framework of a semikinematical<br />

scattering theory. We have analysed reflectivity curves<br />

for lipids POPC (1-Palmitoyl-2-Oleoyl-sn-Glycero-3-Phosphocholine),<br />

DMPC (1,2-Dimyristoyl-sn-Glycero-3-Phosphatidylcholin, mixture of<br />

POPC/POPS (1-Palmitoyl-2-Oleoyl-sn-Glycero-3-[Phospho-L-Serine]) )

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