Abstract
c Theory, experimental aspects, and use in structure calculation of cross-correlated relaxation rates measured on zeroand doublequantum coherences in liquid state NMR are presented. The relative size of the interaction depends on the projection angle between the two tensorial interactions. The tensorial interaction can be either a dipolar interaction or a chemical shift anisotropy relaxation mechanism (CSA). Effects of additional sources of relaxation on the cross-correlated relaxation rates are analyzed. Also, an easy-to-use formalism is given to manipulate different cross-correlated relaxation interactions. The application addresses measurement of the backbone angle c in a protein by measuring dipole(N–H)–dipole(C–H) and CSA(N)–dipole(C– H) cross-correlated relaxation rates. It is shown that ambiguities due to the 3 cosu-1 dependence of one cross-correlated relaxation rate can be overcome by measuring additional cross-correlated relaxation rates. The use of cross-correlated relaxation rates is demonstrated in structure calculations. © 2000 Academic Press
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