Structural highlights
Function
YIAD_ECOLI Suppresses temperature-sensitive mutations in BamB when overexpressed.
Publication Abstract from PubMed
Accurate determination of protein structure by NMR spectroscopy is challenging for larger proteins, for which experimental data are often incomplete and ambiguous. Evolutionary sequence information together with advances in maximum entropy statistical methods provide a rich complementary source of structural constraints. We have developed a hybrid approach (evolutionary coupling-NMR spectroscopy; EC-NMR) combining sparse NMR data with evolutionary residue-residue couplings and demonstrate accurate structure determination for several proteins 6-41 kDa in size.
Protein structure determination by combining sparse NMR data with evolutionary couplings.,Tang Y, Huang YJ, Hopf TA, Sander C, Marks DS, Montelione GT Nat Methods. 2015 Jun 29. doi: 10.1038/nmeth.3455. PMID:26121406[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tang Y, Huang YJ, Hopf TA, Sander C, Marks DS, Montelione GT. Protein structure determination by combining sparse NMR data with evolutionary couplings. Nat Methods. 2015 Jun 29. doi: 10.1038/nmeth.3455. PMID:26121406 doi:http://dx.doi.org/10.1038/nmeth.3455
