Journal
FEBS JOURNAL
Volume 285, Issue 2, Pages 357-371Publisher
WILEY
DOI: 10.1111/febs.14345
Keywords
contrast matching; deuteration; membrane proteins; SANS; Small-angle neutron scattering
Categories
Funding
- Danish Agency for Science, Technology and Innovation funding agency
- Lundbeck Foundation
- Danish Council for Independent Research - Medical Sciences
- GluTarget
- Center for Synthetic Biology (bioSYNergy)
- UCPH Excellence Programme for Interdisciplinary Research
- Lundbeck foundation BRAIN-STRUC project
- National Collaborative Research Infrastructure Strategy - an initiative of the Australian Government
- Lundbeck Foundation [R155-2015-2666, R248-2016-2518] Funding Source: researchfish
- Novo Nordisk Fonden [NNF15OC0016670] Funding Source: researchfish
- Villum Fonden [00007523] Funding Source: researchfish
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A novel and generally applicable method for determining structures of membrane proteins in solution via small-angle neutron scattering (SANS) is presented. Common detergents for solubilizing membrane proteins were synthesized in isotope-substituted versions for utilizing the intrinsic neutron scattering length difference between hydrogen and deuterium. Individual hydrogen/deuterium levels of the detergent head and tail groups were achieved such that the formed micelles became effectively invisible in heavy water (D2O) when investigated by neutrons. This way, only the signal from the membrane protein remained in the SANS data. We demonstrate that the method is not only generally applicable on five very different membrane proteins but also reveals subtle structural details about the sarco/endoplasmatic reticulum Ca2+ ATPase (SERCA). In all, the synthesis of isotope-substituted detergents makes solution structure determination of membrane proteins by SANS and subsequent data analysis available to nonspecialists.
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