The direct determination of protein structure by NMR without assignment
Tóm tắt
Assignment of the resonances in nuclear magnetic resonance spectra is considered a pre‐requisite for the interpretation of spectra that yield structural information. The determination of the three‐dimensional structure of a biological macromolecule may, however, be achieved directly without spectral assignment, using the same set of heteronuclear scalar and dipolar coupling experiments as normally used. A cross‐peak in any of the spectra may be interpreted as a distance between atoms, yielding a set of distances between unassigned atoms that serves to define the tertiary structure of the molecule. The principle is illustrated using the 76 amino acid protein ubiquitin.
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