Eric Lindner

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Assay systems based on the ToxR protein are widely used to investigate interaction of transmembrane domains that come from natural proteins or are isolated from combinatorial libraries. The principle of this method is that self-interaction of any given transmembrane domain, which is expressed within a ToxR chimeric protein, drives ToxR-ToxR assembly in a(More)
The principles underlying the folding of integral membrane proteins are uncovered in an increasingly detailed way. Experimental determination of high-resolution structures followed by analysis of packing reveal structural similarities as well as differences to soluble globular proteins. At the same time, protein/protein interactions at the level of(More)
An oligo-leucine sequence has previously been shown to function as an artificial transmembrane segment that efficiently self-assembles in membranes and in detergent solution. Here, a novel technique, asparagine-scanning mutagenesis, was applied to probe the interface of the self-assembled oligo-leucine domain. This novel approach identifies interfacial(More)
The ToxR transcription activator system is a genetic tool widely used to examine homotypic interactions of alpha-helical transmembrane domains that drive or support oligomerization of integral membrane proteins. Here, we present a variant of this system that was developed to investigate heterotypic interactions. In this system, a homotypically interacting(More)
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