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Andreas STADLER (Forschungszentrum Julich)Poster
Scattering studies are among the few methods that can be used to analyze the structure and dynamics of phospholipid membranes at nanometer scales. However, the available structural information is indirect, as it consists of correlation functions: space-correlation functions for elastic scattering (e.g. SAXS or SANS), and space-time correlation functions for inelastic scattering (e.g. NSE). An...
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Ralf BIEHL (Forschungszentrum Jülich)Oral
A fundamental feature of the antibody structure is the flexible linker between the 3 fragments that allows great flexibility and simultaneous binding to epitopes of antigens and receptors. Combining dynamic light scattering, neutron spin-echo spectroscopy and PFG-NMR we determine characteristic internal fragment dynamics on top of translational and rotational diffusion under crowding...
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Tatsuhito MATSUO (Hiroshima International University)Invited
A hallmark of amyloidosis such as Alzheimer’s disease is the deposition of amyloid fibrils, which are self-assembled protein filaments with core regions rich in β-sheets, in various organs. Cytotoxicity underlying the pathogenesis of amyloidosis is partly caused by the disruption of cell membranes by binding of amyloid fibrils. Since amyloidogenic proteins form polymorphic fibrils with...
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Theresa BOSSERHOFF (JCNS-1 & ILL)Poster
Light is an important stimulus for many biological processes. While structural changes in photo-responsive proteins are studied using well-established techniques, the implications of dynamic transitions during the photo-switching process remain to be assessed. High-resolution neutron backscattering spectroscopy enables the study of protein dynamics on the pico- to nanosecond timescale.
In...
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Olaf HOLDERER (Forschungszentrum Jülich GmbH, JCNS at MLZ)Oral
Emulsions are an indispensable part of everyday life; they are used in a wide range of applications, including cosmetics, drug delivery, and food systems. Mixed interfaces in emulsions are common and are composed of proteins and low molecular weight emulsifiers like phospholipids.
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The charge and nature of phospholipid head groups exert a significant influence on the interfacial structure and... -
Finn SOMBRUTZKI (IBS and ILL Grenoble)Poster
Tau is an intrinsically disordered protein (IDP) expressed in neurons. In contrary to well-folded proteins, IDPs lack a distinct stable 3D structure and sample a vast conformational space instead. Tau’s biological function lays in its interaction with the microtubules. In patients with Alzheimer’s disease, however, it is found to be part of protein filaments in the brain.
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Solutions of tau can...
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