Abstract
Here we describe a new algorithm for automatically determining the mainchain sequential assignment of NMR spectra for proteins. Using only the customary triple resonance experiments, assignments can be quickly found for not only small proteins having rather complete data, but also for large proteins, even when only half the residues can be assigned. The result of the calculation is not the single best assignment according to some criterion, but rather a large number of satisfactory assignments that are summarized in such a way as to help the user identify portions of the sequence that are assigned with confidence, vs. other portions where the assignment has some correlated alternatives. Thus very imperfect initial data can be used to suggest future experiments.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 281-298 |
| Number of pages | 18 |
| Journal | Journal of Biomolecular NMR |
| Volume | 46 |
| Issue number | 4 |
| DOIs | |
| State | Published - Apr 2010 |
Funding
Acknowledgments E.R.P.Z. acknowledges support from NIH grants GM063027 and GM063027-08S1 (E.R.P.Z., PI) and NS059690 (J.E. Gestwicki, PI). We thank Drs. A.V. Kurochkin and D.S. Weaver for the preparation of the Hsc70 NMR samples.
Keywords
- Automatic assignment
- Generic spin system
- Large proteins
- Triple resonance
ASJC Scopus subject areas
- Biochemistry
- Spectroscopy