Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8328216 | International Journal of Biological Macromolecules | 2018 | 25 Pages |
Abstract
Our data indicate that the C-terminal fragment of Ubb+1 is overall highly flexible, except for a short stretch which appears less solvent-exposed. While influencing the hydrodynamic properties of the globular domain, the fragment does not establish long-lived interactions with the globular domain. It results that the structure and stability of Ub are minimally perturbed by the peptide extension. However, binding to UBA2 and to membrane mimics are both affected, exemplifying possible changes in biomolecular recognition experienced by the disease-associated Ubb+1 compared to the wild-type protein.
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Authors
Francesca Munari, Andrea Bortot, Michael Assfalg, Mariapina D'Onofrio,