The direct determination of protein structure by NMR without assignment

FEBS Letters - Tập 510 - Trang 1-4 - 2002
R.Andrew Atkinson1, Vladimı́r Saudek2
1UPR 9004 du CNRS, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, 67400 Illkirch, France
27 Au Canal, 67300 Schiltigheim, France

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.

Tài liệu tham khảo

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FEBS Letters

Tập 510

1-4

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