Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks.

ABSTRACT: The architecture of membrane proteins in their native environment of the phospholipid bilayer is critical for understanding physiological function, but has been difficult to realize experimentally. In this communication we describe the incorporation of a membrane-anchored protein into a supported phospholipid bilayer. Cytochrome P450 2B4 solubilized and purified from the hepatic endoplasmic reticulum was incorporated into phospholipid bilayer nanostructures and oriented on a surface for visualization by atomic force microscopy. Individual P450 molecules were observed protruding from the bilayer surface. Problems associated with deformation of the protein by the atomic force microscopy probe were avoided by analyzing force-dependent height measurements to quantitate the height of the protei

SUBMITTER: Bayburt TH 

PROVIDER: S-EPMC124470 | biostudies-literature | 2002 May

REPOSITORIES: biostudies-literature