The direct determination of protein structure by NMR without assignment

FEBS Letters

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