Abstract
1H NMR saturation transfer and nuclear Overhauser effect (NOE) measurements have been used together with two-dimensional spectra to complete the assignment of the well resolved hyperfine shifted resonances in the spectrum of horse ferricytochrome c and obtain their shifts in the reduced protein. New assignments include the β-CH 2 protons of Met-80, both ring protons of His-18, and the α-CH 2 of Gly-29 and δ-CH 2 of Pro-30, which resonate surprisingly far upfield despite the absence of any Fermi contact contribution to the shift.
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