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Carpe Diubiquitin
Author(s) -
Martin Langdon J.,
Raines Ronald T.
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201005946
Subject(s) - ubiquitin , ubiquitins , lysine , chemistry , residue (chemistry) , nitrogen atom , stereochemistry , deubiquitinating enzyme , ubiquitin ligase , biochemistry , organic chemistry , ring (chemistry) , amino acid , gene
Chained melody : Ubiquitination is forged through the nonstandard isopeptide bond between the ε‐nitrogen atom of a lysine residue on a target protein and the C‐terminal carboxy group of ubiquitin. Several complementary synthetic approaches have led to designated diubiquitin chains in quantities useful for structure–function analyses, culminating in the total chemical synthesis of all seven diubiquitin chains.