Journal
PROTEIN SCIENCE
Volume 23, Issue 5, Pages 662-667Publisher
WILEY-BLACKWELL
DOI: 10.1002/pro.2450
Keywords
ubiquitin; K0-Ub; NMR; CS-Rosetta
Categories
Funding
- Intramural Research Program of the National Institutes of Health
- National Cancer Institute
- Center for Cancer Research
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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 N-15 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. PDB Code(s):
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