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Synthesis of Native Proteins by Chemical Ligation
Abstract
▪ Abstract In just a few short years, the chemical ligation of unprotected peptide segments in aqueous solution has established itself as the most practical method for the total synthesis of native proteins. A wide range of proteins has been prepared. These synthetic molecules have led to the elucidation of gene function, to the discovery of novel biology, and to the determination of new three-dimensional protein structures by both NMR and X-ray crystallography. The facile access to novel analogs provided by chemical protein synthesis has led to original insights into the molecular basis of protein function in a number of systems. Chemical protein synthesis has also enabled the systematic development of proteins with enhanced potency and specificity as candidate therapeutic agents.
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Cited by
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Sletten, E. M., & Bertozzi, C. R. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200900942 · Cited by 3,165
Adding New Chemistries to the Genetic Code
Liu, C. C., & Schultz, P. G. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.105824 · Cited by 1,725
An Expanded Eukaryotic Genetic Code
Chin, J. W., Cropp, T. A., Anderson, J. C., Mukherji, M., Zhang, Z., & Schultz, P. G. (2003) · Science · doi:10.1126/science.1084772 · Cited by 820
Solid-phase peptide synthesis: from standard procedures to the synthesis of difficult sequences
Coin, I., Beyermann, M., & Bienert, M. (2007) · Nature Protocols · doi:10.1038/nprot.2007.454 · Cited by 638
Szkudlinski, M. W., Fremont, V., Ronin, C., & Weintraub, B. D. (2002) · Physiological Reviews · doi:10.1152/physrev.00031.2001 · Cited by 458
Metadata
- Authors
- Dawson, P. E., & Kent, S. B. H.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2000-06
- Volume
- 69
- Issue
- 1
- Pages
- 923-960
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2166405062
- Cited by
- 1,082
- References
- 0
- FWCI
- 1.91
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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