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|1d3z, 10 NMR models ()|
UBIQUITIN NMR STRUCTURE
The refinement of protein structures determined by nuclear magnetic resonance spectroscopy against database potentials of mean force allows for the exclusion of unfavourable conformations of the protein backbone during a structure calculation, resulting in protein structures with a marked improvement in Ramachandran statistics. In this communication, we use multiple sets of residual dipolar couplings as quality assessment criteria for several proteins and show that not only do the Ramachandran and structural quality statistics improve, but a significant improvement in the accuracy of structures is achieved upon refinement.
Validating the use of database potentials in protein structure determination by NMR., Mertens HD, Gooley PR, FEBS Lett. 2005 Oct 24;579(25):5542-8. Epub 2005 Sep 27. PMID:016219311
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Mertens HD, Gooley PR. Validating the use of database potentials in protein structure determination by NMR. FEBS Lett. 2005 Oct 24;579(25):5542-8. Epub 2005 Sep 27. PMID:16219311 doi:10.1016/j.febslet.2005.09.017
- Dikic I, Wakatsuki S, Walters KJ. Ubiquitin-binding domains - from structures to functions. Nat Rev Mol Cell Biol. 2009 Oct;10(10):659-71. PMID:19773779 doi:10.1038/nrm2767