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Direct measurement of the 15N CSA/dipolar relaxation interference from coupled HSQC spectra |
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| Authors: | Hall Jennifer B Dayie Kwaku T Fushman David |
| Institution: | (1) Department of Chemistry and Biochemistry, Center of Biomolecular Structure and Organization, University of Maryland, 1115 Agriculture/Life Science Surge Bldg., College Park, MD, 20742-3360, U.S.A;(2) Department of Molecular Biology, Center for Structural Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH, 44195, U.S.A |
| Abstract: | Here we propose a method for the measurement of the 15N CSA/dipolar relaxation interference based on direct comparison of the 15N doublet components observed in a 1H-coupled 1H-15N HSQC-type spectrum. This allows the determination of the cross-correlation rates with no need for correction factors associated with other methods. The signal overlap problem of coupled HSQC spectra is addressed here by using the IPAP scheme (Ottiger et al., 1998). The approach is applied to the B3 domain of protein G to show that the method provides accurate measurements of the 15N CSA/dipolar cross-correlation rates. |
| Keywords: | chemical shift anisotropy coupled HSQC cross-correlation IPAP method relaxation interference |
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