Formation and Cooperative Behaviour of Protein Complexes on the Cell Membrane
Formation and Cooperative Behaviour of Protein Complexes on the Cell Membrane
With the aim of providing a deeper insight into possible mechanisms of biological self-organization, this thesis presents new approaches to describe the process of self-assembly and the impact of spatial organization on the function of membrane proteins, from a statistical physics point of view. It focuses on three important scenarios: the assembly of membrane proteins, the collective response of mechanosensitive channels and the function of the twin arginine translocation (Tat) system. Using methods from equilibrium and non-equilibrium statistical mechanics, general conclusions were drawn that demonstrate the importance of the protein-protein interactions. Namely, in the first part a general aggregation dynamics model is formulated, and used to show that fragmentation crucially affects the efficiency of the self-assembly process of proteins. In the second part, by mapping the membrane-mediated forces into a simplified many-body system, the dynamic and equilibrium behaviour of interacting mechanosensitive channels is derived, showing that protein agglomeration strongly impacts its desired function. The final part develops a model that incorporates both the agglomeration and transport function of the Tat system, thereby providing a comprehensive description of this self-organizing process.
Collective Response of Self-organised Clusters of Mechanosensitive Channels
Assembly and Fragmentation of Tat Pores
Conclusion.
From the contents:<br />Introduction
The Role of Fragmentation on the Formation of Homomeric Protein ComplexesCollective Response of Self-organised Clusters of Mechanosensitive Channels
Assembly and Fragmentation of Tat Pores
Conclusion.
Guseva, Ksenia
ISBN | 9783642239885 |
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Artikelnummer | 9783642239885 |
Medientyp | E-Book - PDF |
Auflage | 2. Aufl. |
Copyrightjahr | 2011 |
Verlag | Springer-Verlag |
Umfang | 80 Seiten |
Abbildungen | w. 46 ill., 20 col. ill. |
Sprache | Englisch |
Kopierschutz | Digitales Wasserzeichen |