A novel experiment for the quantitative measurement of CSA(1H(N))/CSA(15N) cross-correlated relaxation in 15N-labeled proteins.
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.
Tessari
M
M
Nijmegen SON Research Center, Department of Biophysical Chemisty, University of Nijmegen, The Netherlands. marco@nmr.kun.nl
Vuister
G W
GW
D048868:Adaptor Proteins, Signal Transducing; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry; D047908:Intracellular Signaling Peptides and Proteins; D051379:Mice; D008956:Models, Chemical; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010750:Phosphoproteins / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012015:Reference Standards
D048868:Adaptor Proteins, Signal Transducing; D000596:Amino Acids; D002135:Calcium-Binding Proteins; C082729:Eps15 protein, mouse; D047908:Intracellular Signaling Peptides and Proteins; D009587:Nitrogen Isotopes; D010750:Phosphoproteins; D011506:Proteins