Ellen C Minnihan1, Kenichi Yokoyama1 and JoAnne Stubbe
1, 2
1Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139-4307, USA
2Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139-4307, USA
* Corresponding author: JoAnne Stubbe (stubbe@mit.edu)
F1000 Biology Reports 2009, 1:88
(doi: 10.3410/B1-88)
Published: 26/11/2009 © 2009 Faculty of 1000 Ltd
The electronic version of this article is the complete one and can be found at: http://F1000.com/Reports/Biology/content/1/88
Considerable effort has been dedicated to the development of technology for the site-specific incorporation of unnatural amino acids into proteins, with nonsense codon suppression and expressed protein ligation emerging as two of the most promising methods. Recent research advances in which these methods have been applied to study protein function and mechanism are briefly highlighted, and the potential of the methods for efficient, widespread future use in vitro and in vivo is critically evaluated.