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- W2093394057 abstract "The full utilization of the information contained in protein NMR spectra requires the assignment of resonances to specific residues. Many one-dimensional and twodimensional NMR experiments can be used to give assignments to amino acid type (1-5) but, with the exception of relatively small proteins, assignments to specific residues can only be obtained by the use of chemical modification or from prior knowledge of the three-dimensional structure of the protein. In some cases, such considerations lead to a considerable simplification of the assignment procedure. A simplification is also possible where the study requires the protein to be compared in two or more different states, such as the native or nonnative states (6, 7) or the ligand-free and ligand-bound states (8). In such cases, provided the spectrum of one of the states has been previously characterized and there is exchange between the two states, the spectrum of the second state can be assigned. Tuna cytochrome c is a heme-containing electron transfer protein of 103 amino acids that may exist in either a diamagnetic oxidation state, ferrocytochrome c or a paramagnetic oxidation state, ferricytochrome c. The iron is low-spin in both oxidation states, and in ferricytochrome c it acts as a shift probe with a highly anisotropic magnetic moment. Consequently, the NMR spectra of ferricytochrome c and ferrocytochrome care very different (9). Because of the paramagnetism of ferricytochrome c, its ‘H NMR spectrum is relatively well resolved, and this has allowed resonances of approximately 45% of its carbon-bonded protons to be specifically assigned using a combination of one-dimensional NMR techniques and specific chemical modification (IO, 1Z). In contrast, the ‘H NMR spectrum of ferrocytochrome c has a considerably smaller chemical-shift dispersion, which allows fewer selective double-resonance experiments, and consequently there are fewer specific assignments available. In the present communication, making use of the assignments of ferricytochrome c, we demonstrate the utility of chemical exchange NMR to assign the corresponding resonances of ferrocytochrome c. An equimolar mixture of ferricytochrome c (CIII) and ferrocytochrome c (CII) undergoes electron exchange according to km *c111 + CII z=t *c11 + CIII. ill" @default.
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- W2093394057 date "1984-07-01" @default.
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- W2093394057 title "Correlation of proton chemical shifts in proteins using two-dimensional exchange correlated spectroscopy" @default.
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- W2093394057 doi "https://doi.org/10.1016/0022-2364(84)90159-8" @default.
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