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Lysine-free ubiquitin (K0-Ub) is commonly used to study the ubiquitin-signaling pathway, where it is assumed to have the same structure and function as wild-type ubiquitin (wt-Ub). However, the K0-Ub 15 N heteronuclear single quantum correlation NMR spectrum differs significantly from wt-Ub and the melting temperature is depressed by 19 degrees C, raising the question of the structural integrity and equivalence to wt-Ub. The three-dimensional structure of K0-Ub was determined by solution NMR, using chemical shift and residual dipolar coupling data. K0-Ub adopts the same backbone structure as wt-Ub, and all significant chemical shifts can be related to interactions impacted by the K to R mutations.
Solution structure of lysine-free (K0) ubiquitin.,Huang T, Li J, Byrd RA Protein Sci. 2014 Mar 3. doi: 10.1002/pro.2450. PMID:24591328[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Huang T, Li J, Byrd RA. Solution structure of lysine-free (K0) ubiquitin. Protein Sci. 2014 Mar 3. doi: 10.1002/pro.2450. PMID:24591328 doi:http://dx.doi.org/10.1002/pro.2450
