Assignment of NMR spectra of proteins using triple-resonance two-dimensional experiments.
Two-dimensional versions of HNCA and HNCO experiments are described, which provide essentially the same information as the 3D sequence. A multiple-quantum coherence involving either 15N and 13C alpha or 15N and 13CO is created. One of the two frequencies is given by the middle point between the two cross peaks (zero- and double-quantum) and the other by their separation. Quadrature detection can be performed on either nucleus, modifying only the appearance of the 2D spectrum, but not the information content. These experiments, named MQ-HNCA and MQ-HNCO, are illustrated on a (15N, 13C) doubly labelled cytochrome c2 from Rhodobacter capsulatus (116 amino acids).
Institut de Biologie Structurale, CNRS-CEA, Grenoble, France.
J P
JP
Simorre
B
B
Brutscher
M S
MS
Caffrey
D
D
Marion
D002247:Carbon Isotopes; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008433:Mathematics; D009587:Nitrogen Isotopes; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011506:Proteins; D006859:Hydrogen