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Molecular Orientation Distributions in Protein Films. 2. Site-Directed Immobilization of Yeast Cytochrome c on Thiol-Capped, Self-Assembled Monolayers
- Source :
- Journal of the American Chemical Society. 119:571-576
- Publication Year :
- 1997
- Publisher :
- American Chemical Society (ACS), 1997.
-
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 distribution. 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 ...
- Subjects :
- chemistry.chemical_classification
Total internal reflection fluorescence microscope
biology
Cytochrome c
Self-assembled monolayer
General Chemistry
Linear dichroism
Biochemistry
Catalysis
chemistry.chemical_compound
Crystallography
Colloid and Surface Chemistry
chemistry
Monolayer
Thiol
biology.protein
Heme
Cysteine
Subjects
Details
- ISSN :
- 15205126 and 00027863
- Volume :
- 119
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society
- Accession number :
- edsair.doi...........6c46904beb03f7a67cfc07cc32621bdf
- Full Text :
- https://doi.org/10.1021/ja9623673