Journal
CHEMICAL COMMUNICATIONS
Volume 58, Issue 31, Pages 4913-4916Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1cc07193a
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Funding
- NIH [R35 GM139572]
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In this study, the membrane-anchored flavin mononucleotide binding domain (FBD) of CYP450 reductase was extracted in E. coli lipid-nanodiscs using charge-free pentyl-inulin polymer. The FBD in nanodiscs showed conformational homogeneity and enabled high-resolution NMR probing. P-31 NMR revealed that the polymer had no preference for any specific E. coli lipids and identified the lipid types in the nanodiscs.
The membrane-anchored flavin mononucleotide binding domain (FBD) of CYP450 reductase was extracted in E. coli lipid-nanodiscs using charge-free pentyl-inulin polymer. FBD in nanodiscs was found to be conformationally homogenous and enabled high-resolution NMR probing. P-31 NMR revealed the polymer's lack of preference for any specific E. coli lipids and identified the lipid-types in nanodiscs.
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