Identification of spin diffusion pathways in proteins by isotope-assisted NMR cross-relaxation network editing.
A new isotope-assisted cross-relaxation editing experiment, [1H-13C]DINE-NOESY[1H-15N]HSQC (DINE=Double INEPT Edited), is proposed. It is based on the selective inversion of CH/CH3 or CH2 protons in the middle of the mixing time. The experiment sorts out the spin diffusion paths according to the principal mediators, either the CH/CH3 or the CH2 protons. This is useful in the structure refinement process, as it enables proper alignment of the aliphatic protons in the vicinity of NH protons.
Juranić
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Department of Biochemistry and Molecular Biology, Mayo Graduate School, Mayo Clinic and Foundation, Rochester, MN 55905, USA.
Zolnai
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Macura
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D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D006801:Humans; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008962:Models, Theoretical; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D014452:Ubiquitins / Q000737:chemistry
D002247:Carbon Isotopes; D011506:Proteins; D014452:Ubiquitins; D006859:Hydrogen