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GDR 2478

LISM  IMM  CNRS

Aix Marseille University

Dynamics and Assembly of membrane proteins

James Sturgis' research group is interested in the dynamics and assembly of membrane proteins. We are interested in how membrane proteins fold and assemble in the membrane to form both stable structures, such as the photosynthetic apparatus, or transient dynamic structures such as signalling plateforms.

To investigate the assembly of membrane proteins we use a combination of different theroetical and experimental techniques. In a series of numerical approaches we are using computer simulations and theoretical analysis to investigate the assembly process at various levels of detail (atomistic, coarse-grained and ultra-coarse grained). While at the experimental level we use spectroscopic, microscopic, molecular biology and synthetic biology methods to analyse the assembly process, both in detergents, in model membranes, and in vivo.

We have a series of biological systems of different complexity and scale that we investigate using these techniques. The first and smallest systems are the trans-membrane helices of receptor tyrosine kinases, and several other single pass membrane proteins. The sequences of these transmembrane helices despite their simplicity appear to encode a complex series of interactions with different partners that can be static or dynamic and are of importance in signalling. The second system is the folding and assembly of the membrane protein Aquaporin Z, from Escherichia coli. This tetrameric water channel is able to fold and assemble into an active form. However very little is known about the rules that govern membrane protein folding and we hope to be able to decode some of these rules by examining different steps in the folding of this protein. The final system is the assembly of the bacterial photosynthetic system. This simple system composed of 3 to 4 intergal membrane complexes is able to assemble into specialise membranes within the bacteria, the morphology and composition of these domains are important for function, and we try to understand why certain proteins assemble into these domains and how their internal structure is determined.

Dynamique et Assemblage des Protéines Membranaires


James Sturgis,
January 2014

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