Abstract
Molecular orientation in films of yeast cytochrome c immobilized via disulfide bonding between cysteine 102 and the thiol tail groups of self-assembled monolayers (SAMs) coated on planar glass substrates was investigated. The orientation distribution of the heme groups in the protein film was determined using a combination of absorption linear dichroism, measured in a planar integrated optical waveguide-attenuated total reflection geometry, and emission anisotropy, measured in a total internal reflection fluorescence geometry. The mean heme tilt angle and angular distribution about the mean were recovered using a Gaussian model for the orientation tribution. These data are the first orientation distribution measurements reported for a protein film immobilized using a site-directed bonding strategy. The results show that the molecular architecture examined in this study does not produce a highly oriented protein film. A significant fraction of the immobilized cytochrome c is nonspecifically adsorbed to the SAM surface, which produces a relatively broad distribution of heme orientations.
Original language | English (US) |
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Pages (from-to) | 571-576 |
Number of pages | 6 |
Journal | Journal of the American Chemical Society |
Volume | 119 |
Issue number | 3 |
DOIs | |
State | Published - Jan 22 1997 |
Externally published | Yes |
ASJC Scopus subject areas
- Catalysis
- General Chemistry
- Biochemistry
- Colloid and Surface Chemistry