Martin-Luther-Universität Halle-Wittenberg

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Ordung des SFB TRR 102
Ordnung SFB TRR 102.pdf (43,8 KB)  vom 14.05.2012


MLU Halle-Wittenberg
Naturwissenschaftliche Fakultät II
Institut für Physik

Telefon: +49 (0) 345 55 25825
Telefax: +49 (0) 345 55 27160

Von-Danckelmann-Platz 4
Raum 2.09
06120 Halle

MLU Halle-Wittenberg
Nat.Fak. II Institut für Physik
Geschäftsstelle SFB/TRR 102
06099 Halle

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SFB-Transregio 102

Polymere unter Zwangsbedingungen: eingeschränkte und kontrollierte molekulare Ordnung und Beweglichkeit

Der SFB Transregio 102 ist ein langfristiges Grundlagen-Forschungsprojekt, das von der als Sprecherhochschule fungierenden Martin-Luther-Universität Halle-Wittenberg gemeinsam mit der Universität Leipzig beantragt wurde und durchgeführt wird.

Der SFB-TRR 102 wird von der DFG gefördert.

1. Förderperiode: 01.07.2011 - 30.06.2015

2. Förderperiode: 01.07.2015 - 30.06.2019

Aktuelle Highlights aus der Forschung

Induction of Chirality in β-Turn Mimetic Polymer Conjugates via Postpolymerization “Click” Coupling

Chirality is one of the most determining principles in chemistry and biology, dominating the assembly of large synthetic and biological macromolecules. Polymers with artificial (geometrical) constraints can - similar to alpha-helices or proteins - fold into well defined helical structures, especially those containing a rigid backbone with limited conformational flexibility. We here report on the transfer of chirality, induced by an artificial beta-turn-mimetic element, which is directly linked to a synthetic (helical) polymer. The distance over which chirality is transferred from the geometrical constraint onto the helicity of the polymers is studied, revealing that transfer of chirality is possible up to three chemical bonds between the helix and the chiral center on the beta-turn element.

Coupling and Decoupling of Rotational and Translational Diffusion of Proteins under Crowding Conditions

Cataract, that is, the loss of vision due to growing opacity of the eye lens, is one of the most frequent deseases with a correspondingly huge social (and economic) impact on humankind. It is associated with either phase separation or denaturation and ensuing aggregation in the concentrated solution of various lens proteins, the so-called crystallins. Our understanding of the molecular underpinnings of these processes is as yet incomplete, and it is one of the goals of project A08 to test in how far amyloid formation may be relevant in this context. As a step towards this goal, the constrained diffusive motion of proteins in such a highly crowded environment should be characterized first. It is well established that the large-scale translational diffusion is governed by the viscosity of the system, in agreement with the Stokes-Einstein relation. However, the applicability of the coresponding Stokes-Einstein-Debye relation for rotational diffusion, which is more localized short-time process, is still poorly understood. Using a combination of NMR and fluorescence spectroscopy techniques, we investigate the (de)coupling of the rotational from the translational diffusion in a series of crowded model proteins, revealing that proteins can span the whole range of phenomena in dependence of their complex mutual interactions.

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