Abstract
An experiment is presented which allows for the quantitative measurement of the relaxation interference between the 1H(N) CSA and 15N CSA interactions in 15N labeled proteins. A constant-time buildup scheme is used to measure the differential relaxation rate, eta, between double-quantum (DQ) and zero-quantum (ZQ) 1H(N)-15N coherences. The CSA/CSA experiment was recorded at three different Bo field strengths. The CSA(1H(N))/CSA(15N) cross-correlation rate was obtained from the linear fit of the measured rate, eta, versus Bo2 for 77 residues of the EH2 domain from mouse Eps15.
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