| 摘要 |
The present invention discloses eight new reduced dimensionality (RD) triple resonance nuclear magnetic resonance (NMR) experiments for measuring chemical shift values of certain nuclei in a protein molecule. The RD 3D <highlight><uline>HA</uline></highlight>,<highlight><uline>CA</uline></highlight>,(CO),N,HN NMR experiment and the RD 3D <highlight><uline>H</uline></highlight>,<highlight><uline>C</uline></highlight>,(C-TOCSY-CO),N,HN NMR experiment are designed to yield "sequential" connectivities, while the RD 3D <highlight><uline>H</uline></highlight>alphabeta,<highlight><uline>C</uline></highlight>alphabeta,CO,HA NMR experiment and the RD 3D <highlight><uline>H</uline></highlight>alphabeta,<highlight><uline>C</uline></highlight>alphabeta,N,HN NMR experiment provide "intraresidue" connectivities. The RD 3D <highlight><uline>H</uline></highlight>,<highlight><uline>C</uline></highlight>,C,H-COSY NMR experiment, the RD 3D <highlight><uline>H</uline></highlight>,<highlight><uline>C</uline></highlight>,C,H-TOCSY NMR experiment, and the RD 2D <highlight><uline>H</uline></highlight>,<highlight><uline>C</uline></highlight>,H-COSY NMR experiment allow one to obtain assignments for aliphatic and aromatic side chain chemical shifts, while the RD 2D <highlight><uline>HB</uline></highlight>,<highlight><uline>CB</uline></highlight>,(CG,CD),HD NMR experiment provide information for the aromatic side chain chemical shifts. In addition, a method of conducting suites of RD triple resonance NMR experiments for high-throughput resonance assignment of proteins and identification of the location of secondary structure elements are disclosed.
|
