Protein Synthesis by Chemical Ligation of Unprotected Peptides in Aqueous Solution
β Scribed by Dr. Michael A. Walker
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 236 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0044-8249
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Development of a novel strategy suitable for the solution synthesis of proteins is described, wherein the entire molecule is assembled from fully protected segments in the size range of about 10 residues. Each segment is designed so as to have a common structure of Boc-peptide-OPac (Pac: phenacyl) a
The ability of the endopeptidase a-chymotrypsin (EC 3.4.21.1) to catalyse the reaction of various N aunprotected di-and tripeptide ester derivatives with H-Leu-NH 2 , and with a series of C-terminal free di-and tripeptides at ΓΏ15 C in frozen aqueous solution was investigated. The enzyme is able to s
Established methodology for the preparation of peptide thioesters requires the use of t-butoxycarbonyl chemistry owing to the lability of thioester linkers to the nucleophilic reagents used in Fmoc solid phase peptide synthesis. Both the greater ease of use and the broad applicability of the method
## Abstract Peptideβoligonucleotide conjugates have frequently been synthesized to improve cellular delivery of antisense or antigene compounds, to allow the immobilization of peptide and protein conjugates on DNA arrays, or to decorate nucleic acid architectures with peptide functions. In such app
Protein synthesis by native chemical ligation has been an effective approach for the synthesis of proteins of moderate size. The utility of this approach for protein synthesis is demonstrated by the synthesis of a transcription factor, Zif 268 that contains three zinc finger domains. This synthesis