FEBS Letters | |
The direct determination of protein structure by NMR without assignment | |
Atkinson, R.Andrew2  Saudek, Vladimı́r1  | |
[1] 7 Au Canal, 67300 Schiltigheim, France;UPR 9004 du CNRS, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, 67400 Illkirch, France | |
关键词: Assignment; Nuclear magnetic resonance; Structure; Ubiquitin; | |
DOI : 10.1016/S0014-5793(01)03208-2 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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