Plenarvorträge - DPG-Tagungen
Plenarvorträge - DPG-Tagungen
Plenarvorträge - DPG-Tagungen
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Arbeitskreis Biologische Physik Freitag<br />
works in Physics and Biology (Springer Verlag Berlin, 1998)<br />
AKB 50.6 Fr 10:30 B<br />
Using Spins to Find Functional Modules of Bio-Molecular Networks<br />
— •Sabine Tornow — Theoretische Physik III, Universitaet<br />
Augsburg, D-86135 Augsburg<br />
Genes and proteins are organized on the basis of their particular mutual<br />
relation, or according to their interaction, in cellular and genetic<br />
networks. These include metabolic or signaling pathways, protein interaction,<br />
regulatory or coexpression networks. Integrating the information<br />
from the different types of networks may lead to the notion of a functional<br />
network and functional modules. To find these modules, we propose<br />
a new technique which is based on collective, multi–body correlations in<br />
a genetic network (a). We calculate the correlation strength of a group of<br />
genes (e.g., in the coexpression network) which were identified as members<br />
of a module in a different network (e.g., in the protein interaction<br />
network) and estimate the probability that this correlation strength was<br />
found by chance. Groups of genes with a significant correlation strength<br />
in different networks have a high probability that they perform the same<br />
function. Here, we propose to evaluate the multi–body correlations applying<br />
the Superparamagnetic approach (b). We compare our method<br />
to the presently applied mean Pearson correlations and show that our<br />
method is more sensitive in revealing functional relationships.<br />
(a)Tornow,S. ,Mewes, H.: Functional modules by relating protein interaction<br />
networks and gene expression, Nucleic Acids Research 31, 6283<br />
(2003)<br />
(b) Blatt, M, Wiseman, M., and Domany, E.: Superparamagnetic clustering<br />
of data. (1996) Phys. Rev. Lett., 76, 3251-5.<br />
AKB 50.7 Fr 10:30 B<br />
Mechanics and Force Generation of a Single Cell in Presence<br />
of Cytoskeleton Structure Modifying Bioactive Lipids. —<br />
•alexandre Micoulet 1 , Joachim P. Spatz 1 , and Thomas Seufferlein<br />
2 — 1 Biophysical Chemistry, University of Heidelberg, 69120<br />
Heidelberg, Germany — 2 Department of Internal Medecin I, University<br />
of Ulm, 89081 Ulm, Germany<br />
In tissues, constantly regulated processes, such as biochemical and mechanical<br />
interactions between a cell and its environment play a major role<br />
in differentiation and gene expression of cells. In contrast, cancer cells<br />
are able to escape to these regulations and migrate through tissues since<br />
their mechanical and adhesion properties change drastically than those<br />
of non-tumor cells. Under physiological conditions, we applied a uniaxial<br />
deformation to a single cell adhering between two parallel glass plates<br />
(microplates). A precise feedback control allowed for measurements at<br />
constant force or constant deformation. Both microplates were functionalized<br />
in order to control cell adhesion. Thus, we manipulated a single<br />
living cell by controlled adhesion and defined external mechanical stress.<br />
We evaluated elasticity and viscosity of different cell types, such as fibroblasts,<br />
human pancreatic cancer cells. In presence of two bioactive lipids,<br />
lysophosphalitidic acid (LPA) and sphingosylphosphorylcholine (SPC),<br />
we analysed the mechanical response of Panc-1 cells. LPA and SPC influenced<br />
the organisation of actin- or keratin-cytoskeleton. E.g., elasticity<br />
of Panc-1 cells decreased in presence of SPC consolidating biological<br />
studies which predicted that SPC could facilitate metastasis.<br />
AKB 50.8 Fr 10:30 B<br />
Fibronectin fiber formation by surface tension on microfabricated<br />
pillar interfaces — •Jens Ulmer, Stefan Graeter,<br />
Wouter Roos, and Joachim Spatz — University of Heidelberg, Institute<br />
for Physical Chemistry, Biophysical Chemistry,<br />
The extracellular matrix (ECM) provides positional and environmental<br />
information for cells which are essential for tissue function. ECM proteins<br />
such as fibronectin (FN), laminin or collagen form distinct protein<br />
networks in vivo that show tissue-specific variation in composition and<br />
architecture. In vivo, FN-matrix assembly is mediated through integrins<br />
which bind FN for forming cell-ECM contacts. FN molecules are then<br />
stretched by cell generated forces. This causes conformational change in<br />
FN molecules and enables FN from solution to bind. Thus, fibrillogenesis<br />
of FN is stimulated and directed by force. We mimicked this force<br />
induced FN assembly into fibers in vitro by stretching surface bound FN<br />
molecules through water surface tension appearing between the surface<br />
of a water drop and the tops of microfabricated pillars. Microfabricated<br />
pillar arrays offer binding points to the ECM molecules which then bridge<br />
the pillars tops by fibre network formation. In addition, micropillar interfaces<br />
are sensitive force sensors which allow quantitative access to<br />
the fiber formation process. The architecture of the resultant structure<br />
showed to depend on concentration of the FN-solution and to be mediated<br />
by forces generated from water surface tensions. Subsequently, the<br />
defined FN-networks offers guiding cues for cell-ECM interactions.<br />
AKB 50.9 Fr 10:30 B<br />
Substrate Dependent Fibronectin Fibrillogenesis of Adherent<br />
Cells — •Tilo Pompe 1,2 , Manfred Bobeth 3 , and Wolfgang<br />
Pompe 3,2 — 1 Institut für Polymerforschung Dresden e.V. — 2 Max-<br />
Bergmann-Zentrum für Biomaterialien Dresden — 3 Institut für<br />
Werkstoffwissenschaft, TU Dresden<br />
Cell-cell and cell-substrate binding is supported by extracellular matrix<br />
proteins like fibronectin. The formation of fibrils from single fibronectin<br />
molecules is a complex process which includes binding of cell<br />
receptors, like integrins, conformational changes of fibronectin by mechanical<br />
forces exerted from the cell, and polymerisation of fibronectin<br />
molecules at newly exposed binding sites. The dependence of fibrillogenesis<br />
on the fibronectin bond strength to the substrate was investigated<br />
on different copolymer surfaces in respect to the characteristic pattern<br />
of the fibronectin fibrils. Additionally, the process of fibrillogenesis was<br />
modelled by Monte-Carlo simulations of the diffusion and aggregation<br />
of integrin-fibronectin complexes, including cytoskeletal forces acting on<br />
the focal adhesions. The resulting pattern was analysed in dependence<br />
on the fibronection-substrate bond strength and compared with the experimental<br />
observations.<br />
AKB 50.10 Fr 10:30 B<br />
Rod-Coil Multiblock Copolymers as a Simple Protein Model:<br />
Some Scaling Arguments — •Christian Nowak and Thomas<br />
Vilgis — MPI f”ur Polymerforschung, Postfach 3148, 55021 Mainz<br />
We consider the behaviour of rod-coil multiblock copolymers by means<br />
of scaling arguments. A rich phase behaviour is found depending on the<br />
quality of the solvent and the strenght of the intermolecular interactions.<br />
The phase behavior is essentially driven by strong attractive interactions<br />
of the rodlike parts which stabilize the rod micelles and the entropy loss<br />
and confinement of the flexible joints. Such systems could serve as a<br />
very simple model for proteins like myoglobin where the helical parts are<br />
modelled by stiff rods which are joined by flexible (chainlike) elements.<br />
AKB 50.11 Fr 10:30 B<br />
First-Passage and Residence Times in a Periodically Driven<br />
Integrate-and-Fire Model — •Michael Schindler, Peter<br />
Talkner, and Peter Hänggi — Institut für Physik, Universität<br />
Augsburg<br />
The stochastic integrate-and-fire model presents a simple model for<br />
the spiking behavior of neurons. In this model a neuron ”fires” if an<br />
Ornstein-Uhlenbeck process crosses a prescibed threshold. After the firing<br />
the process is assumed to be in a refractory state, and from there it<br />
is put back into its initial, active, state.<br />
For short refractory times this process can be characterized by the distribution<br />
of either the first-passage times of the threshold or the residence<br />
times in the active state. We determined the distributions of these times<br />
for the integrate-and-fire model in the presence of a periodic signal. This<br />
is done by solving numerically both the respective Langevin equation<br />
and the equivalent Fokker-Planck equation. The results are compared<br />
with an approximate analytic theory. If the period of the signal is large<br />
compared to the relaxation time of the Ornstein-Uhlenbeck signal and if<br />
the threshold is higher than a few times the noise strength we find theory<br />
and numerics to be in excellent agreement.<br />
AKB 50.12 Fr 10:30 B<br />
Fluorescence intermittency of single CdSe/ZnS quantum<br />
dots: A comparison between organic and water soluble ligand<br />
shells. — •Andrei Yu. Kobitski 1 , Colin D. Heyes 1 , Vladimir<br />
V. Breus 1 , Kirill V. Anikin 1 , and G. Ulrich Nienhaus 1,2 —<br />
1 Department of Biophysics, University of Ulm, D - 89069 Ulm, Germany<br />
— 2 Department of Physics, University of Illinois Urbana-Champaign,<br />
Urbana, IL 61801, USA<br />
Recently, chemically synthesized quantum dots (QDs) are becoming<br />
widely used as fluorescent labels in biophysical and life-science research.<br />
The procedure of preparing organic soluble CdSe/ZnS core/shell QDs<br />
has become well established over the last 10 years and reproducibly<br />
gives monodisperse nanocrystals with high emission quantum yields of<br />
up to 50%. However, the procedure of water solubilization of the particles,<br />
which is needed for bio-related experiments, is not so well deter-