Incorporating 1H chemical shift determination into 13C-direct detected spectroscopy of intrinsically disordered proteins in solution.
Exclusively heteronuclear (13)C-detected NMR spectroscopy of proteins in solution has seen resurgence in the past several years. For disordered or unfolded proteins, which tend to have poor (1)H-amide chemical shift dispersion, these experiments offer enhanced resolution and the possibility of complete heteronuclear resonance assignment at the cost of leaving the (1)H resonances unassigned. Here we report two novel (13)C-detected NMR experiments which incorporate a (1)H chemical shift evolution period followed by (13)C-TOCSY mixing for aliphatic (1)H resonance assignment without reliance on (1)H detection.
O'Hare
Bernie
B
Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA. bvo100@psu.edu
Benesi
Alan J
AJ
Showalter
Scott A
SA
D000465:Algorithms; D002247:Carbon Isotopes / Q000032:analysis / Q000737:chemistry; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008956:Models, Chemical; D011489:Protein Denaturation; D011506:Proteins / Q000032:analysis* / Q000737:chemistry*; D011522:Protons; D012680:Sensitivity and Specificity; D012996:Solutions
D002247:Carbon Isotopes; D011506:Proteins; D011522:Protons; D012996:Solutions