Plenarvorträge - DPG-Tagungen
Plenarvorträge - DPG-Tagungen
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]) )