An on/off resonance rotating frame relaxation experiment to monitor millisecond to microsecond timescale dynamics.
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.
Kim
Seho
S
Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.
Baum
Jean
J
D008280:Magnetics; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry; D012399:Rotation; D013997:Time Factors
D011506:Proteins