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Noncovalent dimerization of ubiquitin
Authors:Liu Zhu  Zhang Wei-Ping  Xing Qiong  Ren Xuefeng  Liu Maili  Tang Chun
Institution: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.
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.
Keywords:dimerization  NMR spectroscopy  paramagnetic relaxation enhancement  protein–protein interactions  ubiquitin
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