SEC-SANS for probing the structure of membrane proteins in match-out deuterated carrier systems
We propose to utilize the SEC-SANS setup at D22 to investigate the full potential of the match-out (MO) deuterated membrane protein carrier systems used in our group. Chemically synthesized deuterated de-tergents and lipids and in vivo deuterated membrane scaffolding proteins allow for obtaining scattering data on membrane proteins in both MO deuterated detergents and NDs. This both improves the infor-mation obtained on the membrane proteins and make the subsequent data analysis much easier. The newly developed SEC-SANS setup at D22 is a key factor in this approach, since the systems under investi-gation are highly delicate, and thus prone to form aggregates, which will be removed by the SEC-column. Furthermore, the SEC-SANS setup may provide valuable structural information about dimers or higher order oligomers which can only be separated by the SEC. In addition to a selection of model protein sys-tems, which serves to evaluate the method, the sodium-hydrogen antiporter, NHE1 will be measured. Structural information about NHE1 in solution is scarce, and high-quality SANS data on this protein in MO deuterated carriers would be of very high value to the field.
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ARLETH Lise; Nicolai Tidemand Johansen; KASSEM Noah; LYCKSELL Marie; MARTEL Anne; PEDERSEN Martin Cramer; PORCAR Lionel and F.G. Tidemand. (2018). SEC-SANS for probing the structure of membrane proteins in match-out deuterated carrier systems. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-940
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