Measurement of Protein Backbone 13CO and 15N Relaxation Dispersion at High Resolution
(English)Manuscript (preprint) (Other academic)
Three-dimensional pulse sequences for the measurement of Carr-Purcell-Meiboom-Gill relaxation dispersions and new methods for co-processing non-uniformly sampled data are presented. The new methodology was validated for the disordered protein IgA and for an SH3 domain from Abp1p in exchange between its free form and bound to a peptide from the protein Ark1p. We show that the results are similar to ones obtained using traditional experiments and that accurate excited state chemical shifts can be determined. Furthermore, we show that jackknife analysis of down sampled spectra yields robust estimates of peak intensities errors, eliminating the need for recording duplicate data points. The methodology should be useful for characterization of millisecond dynamics in small to medium-sized proteins with poorly dispersed spectra.
IdentifiersURN: urn:nbn:se:liu:diva-117070OAI: oai:DiVA.org:liu-117070DiVA: diva2:805350