Premium
The direct determination of protein structure by NMR without assignment
Author(s) -
Atkinson R.Andrew,
Saudek Vladimı́r
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03208-2
Subject(s) - heteronuclear molecule , spectral line , chemistry , macromolecule , molecule , yield (engineering) , nmr spectra database , nuclear magnetic resonance , dipole , crystallography , scalar (mathematics) , molecular physics , protein structure , residual dipolar coupling , computational chemistry , nuclear magnetic resonance spectroscopy , chemical physics , physics , stereochemistry , mathematics , quantum mechanics , biochemistry , geometry , organic chemistry , thermodynamics
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.