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Science 23 May 1997:
Vol. 276. no. 5316, p. 1169
DOI: 10.1126/science.276.5316.1169j
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In nuclear magnetic resonance studies of proteins, angles between bond vectors are usually determined by measuring scalar coupling constants and calibrating them with an empirical curve. However, this approach is constrained to adjacent bonds (that is, torsion angles), and multiple solutions are possible. Reif et al. show that this ambiguity can be reduced by measuring the cross-correlated relaxation rates for the dipolar coupling between the four nuclei that participate in two different bonds. Empirical calibration is not needed, and the bonds need not be adjacent.

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