title: Noncovalent dimerization of ubiquitin.
abstract: Another kind of dynamics: Ubiquitin noncovalently dimerizes with a dissociation constant of approximately 5 mM. 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.
authors: State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, Hubei 430071, China.
authors: Zhu
authors: Z
authors: Liu
authors: Wei-Ping
authors: WP
authors: Zhang
authors: Qiong
authors: Q
authors: Xing
authors: Xuefeng
authors: X
authors: Ren
authors: Maili
authors: M
authors: Liu
authors: Chun
authors: C
authors: Tang
mesh_terms: D007700:Kinetics; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D055503:Protein Multimerization; D025801:Ubiquitin / Q000737:chemistry*
chemical_list: D025801:Ubiquitin