Homo-nuclear 13C J-decoupling in uniformly 13C-enriched solid proteins.
Recently, we reported an analysis of carbon lineshapes in high resolution solid-state NMR spectra of uniformly 13C-enriched amino acids. Application of a 13C J-decoupling protocol during the carbon chemical shift evolution period allowed us to separate the contribution of the second-order dipolar shift from that of the 13C-13C J-coupling interactions to carbon linewidths. In this work, we have extended this approach to microcrystalline proteins. We describe the performance of the J-decoupling sequence applied to remove homo-nuclear 13C J-couplings in the 13C spectra of ubiquitin. Analysis of the J-decoupling efficiency for C(alpha) and carbonyl protein sites showed that a significant gain in resolution can be achieved.
Igumenova
Tatyana I
TI
Department of Chemistry, Columbia University, 3000 Broadway MC 3113, New York, NY 10027, USA.
McDermott
Ann E
AE
D000465:Algorithms; D000596:Amino Acids / Q000032:analysis / Q000737:chemistry; D002247:Carbon Isotopes; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011506:Proteins / Q000032:analysis / Q000737:chemistry; D025801:Ubiquitin / Q000032:analysis* / Q000737:chemistry*
D000596:Amino Acids; D002247:Carbon Isotopes; D011506:Proteins; D025801:Ubiquitin