Abstract
The short and medium-range NOEs that can be obtained from 2D NOE spectra and homonuclear 3D HOHAHA-NOE spectra of the protein parvalbumin III of pike have been compared. An extensive analysis has been made of a 3D HOHAHA-NOE spectrum in lH2O of the cross sections perpendicular to the ω3 axis at the amide resonance frequencies, where most of the sequential connectivities can be found. A single 3D HOHAHA-NOE spectrum resulted in 455 3D cross peaks involving short and medium-range NOEs on which the assignment of 108 amino acids residues could be based. The 3D data set allowed definition of the secondary structure better than was previously possible, by the observation of a series of new medium-range NOEs. In addition, the 3D spectrum indicated that the amino acid sequence of pike parvalbumin III contained an error and that the protein actually consists of 109 amino acid residues rather than 108 as previously thought.
Original language | English |
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Pages (from-to) | 5024-5030 |
Number of pages | 7 |
Journal | Journal of the American Chemical Society |
Volume | 112 |
Issue number | 13 |
DOIs | |
Publication status | Published - Jan 1990 |