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- W66235364 abstract "It is shown that many of the 1 H resonances of a small protein, lysozyme, can be resolved by using very high magnetic fields and computational methods. The complete identification, or assignment, of the resolved resonances is closely linked to knowledge about the structure of the protein in solution. A brief and critical review is presented of assignment methods, including double resonance, multiplet structure measurements, pH titrations, site specific paramagnetic probes, intrinsic paramagnetic centres, solvent exchange, chemical modifications, and the specific binding properties of the protein. It is shown how these methods can be used to assign ( a ) to a particular class of 1 H, e.g. NH or CH, ( b ) to a particular amino acid type and ( c ) to a particular amino acid in the protein." @default.
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- W66235364 date "1975-08-27" @default.
- W66235364 modified "2023-10-17" @default.
- W66235364 title "Assignment of the <sup>1</sup> H n.m.r. spectra of proteins" @default.
- W66235364 cites W603679491 @default.
- W66235364 doi "https://doi.org/10.1098/rspa.1975.0123" @default.
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