Ontology highlight
ABSTRACT:
SUBMITTER: AlTawallbeh G
PROVIDER: S-EPMC5650499 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
AlTawallbeh Ghaith G Haque Mohammad M MM Streletzky Kiril A KA Stuehr Dennis J DJ Bayachou Mekki M
Biochemical and biophysical research communications 20170925 4
Endothelial nitric oxide synthase (eNOS) is a membrane-anchored enzyme. To highlight the potential role and effect of membrane phospholipids on the structure and activity of eNOS, we have incorporated the recombinant oxygenase subunit of eNOS into lipid nanodiscs. Two different size distribution modes were detected by multi-angle dynamic light scattering both for empty nanodiscs, and nanodiscs-bound eNOS<sub>oxy</sub>. The calculated hydrodynamic diameter for mode 1 species was 9.0 nm for empty ...[more]