Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 131, Issue 27, Pages 9480-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja9020233
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Funding
- Wellcome Trust [079819]
- BBSRC [G004668]
- BMRC, Singapore [R154000272305]
- BBSRC [BB/G004668/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G004668/1] Funding Source: researchfish
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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 similar 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 (alpha(7)alpha(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.
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