A 4D HCCH-TOCSY experiment for assigning the side chain 1H and 13C resonances of proteins.
A 4D HCCH-TOCSY experiment is described for correlating and assigning the 1H and 13C resonances of protein amino acid side chains that has several advantages over 3D versions of the experiment. In many cases, both the 1H and 13C chemical shifts can be obtained in the 4D experiment from a simple inspection of the 13C(omega 3), 1H(omega 4) planes extracted at the 1H alpha(omega 1)/13C alpha(omega 2) chemical shifts. Together with the 3D and 4D triple resonance experiments, this allows sequence-specific assignments to be obtained. In addition, the increased resolution of the 4D experiment compared to its 3D counterpart allows automation of resonance assignments.
D002147:Calmodulin / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008836:Micrococcal Nuclease / Q000737:chemistry; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D016559:Tacrolimus / Q000031:analogs & derivatives / Q000737:chemistry
D002147:Calmodulin; D011506:Proteins; C058028:immunomycin; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C031629:phosphoenolpyruvate-glucose phosphotransferase; D008836:Micrococcal Nuclease; D016559:Tacrolimus