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|Title:||Automated assignment in selectively methyl-labeled proteins||Authors:||Xu, Y.
|Issue Date:||15-Jul-2009||Citation:||Xu, Y., Liu, M., Simpson, P.J., Isaacson, R., Cota, E., Marchant, J., Yang, D., Zhang, X., Freemont, P., Matthews, S. (2009-07-15). Automated assignment in selectively methyl-labeled proteins. Journal of the American Chemical Society 131 (27) : 9480-9481. ScholarBank@NUS Repository. https://doi.org/10.1021/ja9020233||Abstract:||(Figure Presented) Specific methyl labeling schemes and transverse relaxation optimized spectroscopy (TROSY) has extended the molecular size range for the application of NMR spectroscopy to very large proteins (up to ∼1 MDa). Existing strategies for resonance assignment of methyl groups in large systems are based on NMR spectra recorded on smaller fragments and mutants. This is very time-consuming, and chemical shift changes due to mutation or truncation can often complicate interpretation. We have developed a new automated procedure able to rapidly assign the majority of methyl groups in very large proteins, without recourse to mutagenesis or truncated fragments (http://nmr.bc.ic.ac.uk/map-xs/). We demonstrate the effectiveness of this approach on the 300 kDa, ILV-labeled proteasome (α7α 7) for which excellent spectra have been previously recorded. Of the observed methyl groups, 99% can be correctly assigned in a matter of minutes without manual intervention. © 2009 American Chemical Society.||Source Title:||Journal of the American Chemical Society||URI:||http://scholarbank.nus.edu.sg/handle/10635/100137||ISSN:||00027863||DOI:||10.1021/ja9020233|
|Appears in Collections:||Staff Publications|
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