Deniz Yuksel - Protein Engineering Using Noncanonical Amino Acids

Version 1

      Publication Details (including relevant citation   information):

      Yuksel, D.; Pamuk, D.; Ivanova, Y.; Kumar, K.   "Protein Engineering Using Noncanonical Amino Acids" in   Protein Engineering and Design Park, S. and Cochran, J.   Eds., Taylor & Francis 2009, invited   chapter, pp 205-222.


      The limited set of structural and chemical functionalities   represented in the side
      chains of the canonical amino acids necessitate   post-translational processing of
      expressed protein products. Such processing combinatorially   expands both the diversity
      and functional attributes of proteins. This suggests that while   the extant set of
      twenty encoded amino acids can support the rudimentary functions   of living systems,
      optimized function requires a larger set. Site directed   mutagenesis has proven to be
      an invaluable tool in tailoring structural features of enzymes   and has allowed detailed scrutiny of function and creation of   enzymatic activities not found in nature. Nevertheless, the   limited set of functional groups available constrains the range   of possible applications. One could envision entirely new   functions for proteins, or even the evolution of entire organisms   endowed with extrabiological properties, if the set of functional   groups present on the side chains can be expanded.

      Schultz and Chamberlin pioneered the incorporation of unnatural   amino acids
      using nonsense codon suppression. More than 150 unnatural amino   acids have been incorporated by this technique both in vitro and   in vivo, allowing interrogation of mechanism and structure in   unsurpassed detail. This chapter focuses on applications made   possible by introducing unnatural amino acids into proteins with   a brief overview of methodologies of incorporation.

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