Original paper

Stability and Conformation of a Chemoreceptor HAMP Domain Chimera Correlates with Signaling Properties

Volume: 112, Issue: 7, Pages: 1383 - 1395
Published: Apr 1, 2017
Abstract
HAMP domains are dimeric, four-helix bundles that transduce conformational signals in bacterial receptors. Genetic studies of the Escherichia coli serine receptor (Tsr) provide an opportunity to understand HAMP conformational behavior in terms of functional output. To increase its stability, the Tsr HAMP domain was spliced into a poly-HAMP unit from the Pseudomonas aeruginosa Aer2 receptor. Within the chimera, the Tsr HAMP undergoes a thermal...
Paper Details
Title
Stability and Conformation of a Chemoreceptor HAMP Domain Chimera Correlates with Signaling Properties
Published Date
Apr 1, 2017
Volume
112
Issue
7
Pages
1383 - 1395
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