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

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