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Accessing posttranslationally modified proteins through thiol positioning
Author(s) -
Kumar K. S. Ajish,
Brik Ashraf
Publication year - 2010
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1229
Subject(s) - native chemical ligation , ligation , chemistry , peptide , chemical ligation , combinatorial chemistry , thiol , posttranslational modification , computational biology , biochemistry , chemical synthesis , biology , microbiology and biotechnology , enzyme , in vitro
The field of peptide synthesis achieved considerable advancement in the last decade with the discovery of native chemical ligation (NCL). With the aim of broader application of ligation methods in the synthesis of proteins several strategies have been developed. One of the significant contributions to NCL based strategies is the desulfurization reaction, which removes the thiol handle to generate the unmodified protein. The principle of NCL coupled with desulfurization is effortlessly executed in the synthesis of posttranslationally modified proteins. This short account will cover the recent developments on how new methods of chemical ligation is being evolved and exploited in achieving posttranslationally modified proteins. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.