| Abstrakt: |
The sequence specific assignment of theH NMR spectrum of barley serine proteinase inhibitor 2 is described. The sequential assignment procedure has been applied to the residues 22 to 83. The 21 residues in the N-terminal part of the structure were shown to be a random coil for which sequential assignment was not immediately possible. For the C-terminal part of the protein starting at Thr-22 and ending with the C-terminal residue Gly-83, sequence specific assignment of all the H, H, H, H resonances was achieved and complete sequence specific assignment of the non labile protons of the amino acid residue types of glycine, alanine, threonine, serine, valine, isoleucine, leucine, asparagine, aspartic acid, glutamine, glutamic acid, phenylalanine, tyrosine and tryptophan is reported. [ABSTRACT FROM AUTHOR] |
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