SASMod: a new methodological approach for ShuA-DDM complex structure modeling
Structural studies of membrane proteins (MPs) are a challenge in biology because they highly depend on the amphiphilic environment (e.g. detergents) hat allow MP stabilization and proper folding. The description of the detergent behavior around a MP (corona steric hindrance, specific interactions with MP) could be useful to select the suitable detergents for MP biochemistry and structural biology. Up to now, detergent modeling was made possible from SAXS data only using the MP atomic 3D-structure. The aim of our project is to propose a methodology when no MP 3D structure is available. We propose to make a proof of principle with ShuA-DDM complex. Based on SEC-SANS measurements, by contrast matching DDM, we will extract an ab initio low-resolution envelop for ShuA alone. With additional SEC-SAXS data of the whole complex, we will adapt MEMPROT or use molecular dynamics simulations to model the detergent corona around ShuA ansd will compare with results from Abel et al BBA 2021.
The data is currently only available to download if you are a member of the proposal team.
The recommended format for citing this dataset in a research publication is in the following format:
Bonneté; COMBET Sophie; MARTEL Anne; PORCAR Lionel and POZZA Alexandre. (2023). SASMod: a new methodological approach for ShuA-DDM complex structure modeling. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-1060
This data is not yet public
This data is not yet public
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