Noncovalent dimerization of ubiquitin

Zhu Liu, Wei Ping Zhang, Qiong Xing, Xuefeng Ren, Maili Liu, Chun Tang

Research output: Contribution to journalArticlepeer-review

69 Scopus citations


Another kind of dynamics: Ubiquitin noncovalently dimerizes with a dissociation constant of approximately 5mM. 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.

Original languageEnglish (US)
Pages (from-to)469-472
Number of pages4
JournalAngewandte Chemie - International Edition
Issue number2
StatePublished - Jan 9 2012
Externally publishedYes


  • NMRspectroscopy
  • dimerization
  • paramagnetic relaxation enhancement
  • protein-protein interactions
  • ubiquitin


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