SEC-SANS for probing the structure of membrane proteins in lipid-protein nanodiscs
During the last five years our group has focused on developing platforms and approaches to enable combined SANS and SAXS based structural studies of membrane proteins under solution conditions. SANS holds a particularly large potential in this context due to the opportunity for H-D based contrast variation. Unfortunately, the 100% D2O based buffers which in theory provides optimal contrast and signal-to-noise, destabilize many proteins and promote aggregation in the experimental samples. These D2O induced aggregation effects have unfortunately been clearly reflected in many of our previous SANS experimental data and often we have had to discard the data. D22 at ILL has recently, as the first neutron user-facility internationally, implemented a so-called size-exclusion chromatography (SEC) setup in the SANS sample environment enabling SEC-SANS. Based on our experience with similar SEC-SAXS setups, we have a strong expectation that this setup will solve the above mentioned problems with D2O-induced aggregation and we here propose an ambitious experiment to investigate membrane proteins relevant for the understanding and treatment of hemophilia.
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ARLETH Lise; HOLM Viktor L; Nicolai Tidemand Johansen; Andreas Haahr Larsen; MARTEL Anne; MIDTGAARD Soren; PORCAR Lionel and SKAR-GISLINGE Nicholas. (2016). SEC-SANS for probing the structure of membrane proteins in lipid-protein nanodiscs. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-885
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