related to degree

• Xie, Jianming, Ph.D. in Chemistry, Scripps Research 2001 - 2006

authors

• Xie, Jianming
• Schultz, Peter

publication date

• July 2005

journal

• Methods  Journal

abstract

• A general method was recently developed that makes it possible to genetically encode unnatural amino acids (UAAs) with diverse physical, chemical or biological properties in Escherichia coli, yeast, and mammalian cells. Over 30 UAAs have been cotranslationally incorporated into proteins with high fidelity and efficiency by means of a unique codon and corresponding tRNA-synthetase pair. A key feature of this methodology is the orthogonality between the new translational components and their endogenous host counterparts. Specifically, the codon for the UAA should not encode a common amino acid; neither the new tRNA nor cognate aminoacyl tRNA synthetase should cross-react with any endogenous tRNA-synthetase pairs; and the new synthetase should recognize only the UAA and not any of the 20 common amino acids. This methodology provides a powerful tool for exploring protein structure and function both in vitro and in vivo, as well as generating proteins with new or enhanced properties.

subject areas

• Amino Acids
• Base Sequence
• Genetic Code
• Molecular Sequence Data
• Nucleic Acid Conformation
• Protein Biosynthesis
• Protein Engineering
• Proteins
• RNA, Transfer

keywords

• directed evolution
• orthogonal tRNA-synthetase pair
• protein engineering
• unnatural amino acid incorporation

International Standard Serial Number (ISSN)

• 1046-2023

Digital Object Identifier (DOI)

• 10.1016/j.ymeth.2005.04.010

PubMed ID

• 16076448

start page

• 227

end page

• 238

volume

• 36

issue

• 3