Abstract
Rotating frame relaxation experiments in proteins are used to study slow motions on the microsecond to millisecond timescale. An on/off resonance rotating frame relaxation experiment (R(1)(rho)) has been developed that incorporates adiabatic rotations into a R(1)(rho)-R(1) constant relaxation time experiment with weak radio frequency field strengths in order to effectively lock the magnetization over a wide range of (15)N frequencies. The new pulse sequence allows the measurement of a wide range of chemical exchange timescales on the order of 1.0 to 0.05 ms over an asymmetric bandwidth from +1.7omega(l) to -0.5omega(l) in a single experiment. A total bandwidth of +/-l.7omega(l) is obtained by performing the experiment a second time with a reversed adiabatic rotation.
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