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Proton nmr assignments and surface accessibility of tryptophan residues in lysozyme using photochemically induced dynamic nuclear polarization spectroscopy



Proton nmr assignments and surface accessibility of tryptophan residues in lysozyme using photochemically induced dynamic nuclear polarization spectroscopy



Biochemistry 22(8): 1906-1911



Tryptophan resonances in the 360-MHz 1H photochemically induced dynamic nuclear polarization spectrum of hen egg white lysozyme are investigated in detail. All resonances of 1 tryptophan, and 6 of another are identified and assigned to their respective protons. The methods employed, all involving nuclear spin polarization, include the study of cross-relaxation effects and the use of selective radio-frequency irradiation, Gd3+ as a paramagnetic probe, and riboflavin as the chemically induced dynamic nuclear polarization generating dye. From a comparison of the experimental results with the known X-ray structure of lysozyme, 2nd-stage assignments of the 2 tryptophan residues (Trp-62 and Trp-123) are proposed. A number of other resonances are characterized, among them Trp-63 C(2)H and 4 indirectly polarized methyl groups.

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