NMR studies of the interaction of gene-V protein of bacteriophage M13 with oligonucleotides.

This paper describes the preparation of deuterated phenylalanine ([2H7]-phenylalanine) and the isolation of phage M13 encoded gene-V protein in which this deuterated amino acid was incorporated. Using this protein spectral assignments of resonances in the aromatic region of the 1H-NMR spectrum of the gene-V protein have been made. Furthermore the interaction of the gene-V protein with the tetranucleotide d(pC-G-C-G) and the hexanucleotide d(pC-G-C-G-C-G) was investigated. From the changes in the aromatic region of the NMR spectrum occurring after binding, it is concluded that at least one phenylalanine and one tyrosine is involved in the interaction with the oligonucleotides via stacking.