Please use this identifier to cite or link to this item: https://doi.org/10.1021/ja9020233
DC FieldValue
dc.titleAutomated assignment in selectively methyl-labeled proteins
dc.contributor.authorXu, Y.
dc.contributor.authorLiu, M.
dc.contributor.authorSimpson, P.J.
dc.contributor.authorIsaacson, R.
dc.contributor.authorCota, E.
dc.contributor.authorMarchant, J.
dc.contributor.authorYang, D.
dc.contributor.authorZhang, X.
dc.contributor.authorFreemont, P.
dc.contributor.authorMatthews, S.
dc.date.accessioned2014-10-27T08:22:25Z
dc.date.available2014-10-27T08:22:25Z
dc.date.issued2009-07-15
dc.identifier.citationXu, 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
dc.identifier.issn00027863
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100137
dc.description.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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/ja9020233
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/ja9020233
dc.description.sourcetitleJournal of the American Chemical Society
dc.description.volume131
dc.description.issue27
dc.description.page9480-9481
dc.description.codenJACSA
dc.identifier.isiut000268239400006
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

28
checked on Jan 31, 2023

WEB OF SCIENCETM
Citations

27
checked on Jan 24, 2023

Page view(s)

223
checked on Jan 26, 2023

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.