Nature employs complex networks of protein-tailoring enzymes to effect the post-translational modification of proteins in vivo. By comparison, modern chemical methods rely upon either nonspecific labeling techniques or upon the genetic incorporation of bioorthogonal handles. To develop truly robust bioconjugates it is necessary to develop methods which possess the exquisite activity and specificity observed in biological catalysts. One attractive strategy to achieve this is the engineering of protein-tailoring enzymes possessing user-defined specificity and high catalytic efficiency. / Chemistry and Chemical Biology
Identifer | oai:union.ndltd.org:harvard.edu/oai:dash.harvard.edu:1/12274116 |
Date | 04 June 2015 |
Creators | Dorr, Brent Matthew |
Contributors | Liu, David Ruchien |
Publisher | Harvard University |
Source Sets | Harvard University |
Language | en_US |
Detected Language | English |
Type | Thesis or Dissertation |
Rights | open |
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