Direct Monitoring of β-Sheet Formation in the Outer Membrane Protein TtoA Assisted by TtOmp85
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Attenuated total reflection Fourier-transform infrared (ATR-FTIR) spectroscopy was applied to investigate the folding of an outer membrane protein, TtoA, assisted by TtOmp85, both from the thermophilic eubacterium Thermus thermophilus. To directly monitor the formation of β-sheet structure in TtoA and to analyze the function of TtOmp85, we immobilized unfolded TtoA on an ATR crystal. Interaction with TtOmp85 initiated TtoA folding as shown by time-dependent spectra recorded during the folding process. Our ATR-FTIR experiments prove that TtOmp85 possesses specific functionality to assist β-sheet formation of TtoA. We demonstrate the potential of this spectroscopic approach to study the interaction of outer membrane proteins in vitro and in a time-resolved manner.
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SCHMID, Katharina, Wolfram WELTE, Karin HAUSER, 2016. Direct Monitoring of β-Sheet Formation in the Outer Membrane Protein TtoA Assisted by TtOmp85. In: Biochemistry. 2016, 55(31), pp. 4333-4343. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/acs.biochem.6b00691BibTex
@article{Schmid2016-08-09Direc-37497, year={2016}, doi={10.1021/acs.biochem.6b00691}, title={Direct Monitoring of β-Sheet Formation in the Outer Membrane Protein TtoA Assisted by TtOmp85}, number={31}, volume={55}, issn={0006-2960}, journal={Biochemistry}, pages={4333--4343}, author={Schmid, Katharina and Welte, Wolfram and Hauser, Karin} }
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