Based on the analysis of the proton-proton distance dependences from the conformational characteristics of the L-amino acid residues, the correlation diagram of the NOE cross peak intensity waited values with the regions of the sterically allowed space (phi, psi) was proposed. The method for determining the dihedral angles phi, psi values using the information about NOE cross peak intensities was elaborated. By the model spectral NMR parameters of the bovine pancreatic trypsin inhibitor, it is shown that the accuracy of the angles phi, psi determination exceed the corresponding accuracy provided by other methods of the structural interpretation of the two-dimensional NMR spectroscopy data. The analysis of the waited spectral NMR parameters for the different types of protein regular secondary structures and beta-turns was performed.
|Translated title of the contribution||Relation between the spectral NMR parameters and conformation characteristics of the amino acid residue backbone. Analysis of elements of the secondary structure of proteins|
|Number of pages||9|
|State||Published - Nov 1987|
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