Hydrogen-1 and carbon-13 nuclear magnetic resonance of the aromatic residues of fd coat protein

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Abstract
The aromatic residues of [phage] fd coat protein in sodium dodecyl sulfate micelles are characterized by 1H and 13C NMR. Resonances from both types of nuclei show structure-induced chemical shift dispersion and line widths indicative of a folded native structure for the protein. The 2 tyrosines were found to have pKa of 12.3 and 12.5 by 1H NMR and spectrophotometric titrations. 13C relaxation measurements show that 2 of the 3 Phe rings have significant internal mobility, the 2 Tyr rings have moderate internal mobility and the Trp side chain is completely immobilized. Qualitative comparisons are made between the intact virus and the isolated coat protein.