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- W2103076293 abstract "Negative phototaxis in Archaea is mediated by the sensory rhodopsin II/transducer complex ( Np SRII/ Np HtrII). After light excitation, the signal is relayed from the receptor to Np HtrII where a rotary motion of TM2 in the membrane domain ( Np HtrII 1–114 ) is induced. This conformational change is transferred to the downstream two‐component signaling cascade. Here, we describe the chemical synthesis of this membrane domain, which consists of the two transmembrane helices TM1 and TM2. Np HtrII 1–114 was synthesized using two sequential ligation steps. The first ligation between Np HtrII 47–59 and Np HtrII 60–114 was performed in organic solvents, whereas the final ligation was successful in an aqueous buffer that contained a detergent and a denaturant. The product was refolded into micelles and showed functional properties as determined by binding studies to its cognate receptor Np SRII and by photocycle experiments. This work demonstrates that membrane proteins can be successfully synthesized by chemical means paving the way for tailor‐made modifications. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd." @default.
- W2103076293 created "2016-06-24" @default.
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- W2103076293 date "2014-01-06" @default.
- W2103076293 modified "2023-10-15" @default.
- W2103076293 title "Total chemical synthesis of a membrane protein domain analogue containing two transmembrane helices: functional reconstitution of the semisynthetic sensory rhodopsin/transducer complex" @default.
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- W2103076293 doi "https://doi.org/10.1002/psc.2605" @default.
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