Enzymatic "Click" Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase
Singled out for special treatment: Naturally occurring glutathione S-transferase (GST) was used to catalyze an efficient "click" ligation between polypeptides with an N-terminal glutathione sequence and biomolecules or chemical probes containing perfluorinated aromatic groups (see scheme)....
Main Authors: | Zhang, Chi (Contributor), Spokoyny, Alexander M. (Contributor), Zou, Yekui (Contributor), Pentelute, Bradley L. (Contributor), Simon, Mark (Contributor) |
---|---|
Other Authors: | Massachusetts Institute of Technology. Department of Chemistry (Contributor) |
Format: | Article |
Language: | English |
Published: |
Wiley Blackwell,
2015-02-25T20:15:29Z.
|
Subjects: | |
Online Access: | Get fulltext |
Similar Items
-
Enzymatic modification of DNA and RNA 3'-termini for click ligation
by: Xiong, Chen
Published: (2014) -
Convergent diversity-oriented side-chain macrocyclization scan for unprotected polypeptides
by: Zou, Yekui, et al.
Published: (2015) -
A Perfluoroaryl-Cysteine S[subscript N]Ar Chemistry Approach to Unprotected Peptide Stapling
by: Spokoyny, Alexander M., et al.
Published: (2015) -
Catalysis and Site-Specific Modification of Glutathione Transferases Enabled by Rational Design
by: Håkansson Hederos, Sofia
Published: (2005) -
The still mysterious roles of cysteine-containing glutathione transferases in plants
by: Pierre-Alexandre eLallement, et al.
Published: (2014-08-01)