| 摘要 |
The present invention discloses eleven reduced dimensionality (RD) triple resonance nuclear magnetic resonance (NMR) experiments for measuring chemical shift values of certain nuclei in a protein molecule, where the chemical shift values encoded in a peak pair of an NMR spectrum are detected in a phase sensitive manner. The RD 3D <u style="single">HA,<u style="single">CA,(CO),N,HN NMR and RD 3D <u style="single">H,<u style="single">C,(C-TOCSY-CO),N,HN NMR experiments are designed to yield "sequential" connectivities, while the RD 3D <u style="single">Halpha/beta,<u style="single">Calpha/beta, CO,HA NMR and RD 3D <u style="single">Halpha/beta,<u style="single">Calpha/beta,N,HN NMR experiments provide "intraresidue" connectivities. The RD 3D <u style="single">H,<u style="single">C,C,H-COSY NMR, RD 3D <u style="single">H,<u style="single">C,C,H-TOCSY NMR, and RD 2D <u style="single">H,<u style="single">C,H-COSY NMR experiments allow one to obtain assignments for aliphatic and aromatic side chain chemical shifts, while the RD 2D <u style="single">HB,<u style="single">CB,(CG,CD),HD NMR experiment provide information for the aromatic side chain chemical shifts. In addition, methods of conducting suites of RD triple resonance NMR experiments for high-throughput resonance assignment of proteins and determination of secondary structure elements are disclosed.
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