Journal
ANNUAL REVIEW OF BIOCHEMISTRY
Volume 73, Issue -, Pages 147-176Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biochem.73.012803.092429
Keywords
aminoacyl-tRNA synthetase; suppression; orthogonal; protein biosynthesis
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Funding
- NCI NIH HHS [CA92577] Funding Source: Medline
- NIGMS NIH HHS [GM23562, GM15539] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA092577] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM023562, R01GM015539, R37GM015539] Funding Source: NIH RePORTER
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The genetic code is established by the aminoacylation of transfer RNA, reactions in which each amino acid is linked to its cognate tRNA that, in turn, harbors the nucleotide triplet (anticodon) specific to the amino acid. The accuracy of aminoacylation is essential for building and maintaining the universal tree of life. The ability to manipulate and expand the code holds promise for the development of new methods to create novel proteins and to understand the origins of life. Recent efforts to manipulate the genetic code have fulfilled much of this potential. These efforts have led to incorporation of nonnatural amino acids into proteins for a variety of applications and have demonstrated the plausibility of specific proposals for early evolution of the code.
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