title: Unveiling the Structural and Dynamic Nature of the Ubiquitin Code.
abstract: In this issue of Structure, Castañeda et al. (2016b) use multi-disciplinary approaches including NMR techniques, small-angle neutron scattering, and docking to convincingly demonstrate that K27-linked diubiquitin is relatively rigid with unexpected similarity to the conformation of K48-linked diubiquitin bound to the UBA2 domain of hHR23a.
authors.affiliation: Department of Protein Chemistry & Structural Biology, Genentech, Inc., 1 DNA Way, South San Francisco, CA 94080, USA.
authors.forename: Paola
authors.initials: P
authors.lastname: Di Lello
authors.affiliation: Department of Protein Chemistry & Structural Biology, Genentech, Inc., 1 DNA Way, South San Francisco, CA 94080, USA. Electronic address: hymowitz@gene.com.
authors.forename: Sarah G
authors.initials: SG
authors.lastname: Hymowitz
mesh_terms: D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D053838:Scattering, Small Angle; D025801:Ubiquitin / Q000737:chemistry*; D014452:Ubiquitins / Q000737:chemistry
chemical_list: D025801:Ubiquitin; D014452:Ubiquitins