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Noncovalent Dimerization of Ubiquitin
Author(s) -
Liu Zhu,
Zhang WeiPing,
Xing Qiong,
Ren Xuefeng,
Liu Maili,
Tang Chun
Publication year - 2012
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.201106190
Subject(s) - ubiquitins , ubiquitin , ubiquitin ligase , deubiquitinating enzyme , ubiquitin conjugating enzyme , protein subunit , chemistry , dimer , covalent bond , biochemistry , biophysics , microbiology and biotechnology , stereochemistry , biology , gene , organic chemistry
Another kind of dynamics : Ubiquitin noncovalently dimerizes with a dissociation constant of approximately 5 m M . The two subunits adopt an array of relative orientations, utilizing an interface also for binding to other proteins (see picture). Quaternary fluctuation among members of the dimer ensemble constitutes a different kind of dynamics that complements the tertiary dynamics of each ubiquitin subunit.