Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1317089 | Journal of Inorganic Biochemistry | 2007 | 7 Pages |
Abstract
De novo proteins from designed combinatorial libraries were bound to heme terminated gold electrodes. The novel heme proteins were shown to possess peroxidase activity, and this activity was compared to that of horseradish peroxidase and bovine serum albumin when immobilized in a similar fashion. The various designed proteins from the libraries displayed distinctly different levels of peroxidase activity, thereby demonstrating that the sequence and structure of a designed protein can exert a substantial effect on the peroxidase activity of immobilized heme.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Aditi Das, Michael H. Hecht,