title: An Off-resonance Rotating Frame Relaxation Experiment for the Investigation of Macromolecular Dynamics Using Adiabatic Rotations
abstract: 15N off-resonance rotating frame relaxation can be applied to the study of internal dynamics in proteins in the millisecond to microsecond regime. We show that the performance of existing methods can be improved by application of simultaneous amplitude and phase-modulated adiabatic RF pulses to align the nuclear spin magnetization with the off-resonance spin-lock field for all the spins under investigation. Application of this technique to the 269-residue serine protease PB92 allowed the measurement of 15N off-resonance rotating frame relaxation rates for all nonoverlapping residues in the protein, including the arginine side chains, encompassing a chemical shift range of 50 ppm. Simulations indicate that by use of the proposed adiabatic RF pulses rotating frame relaxation rates can be obtained for magnetization vectors aligned at arbitrary angles with the static field. Copyright 1998 Academic Press.
authors.affiliation: Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, Utrecht, 3584 CH, The Netherlands
authors.initials: FAA
authors.lastname: Mulder
authors.lastname: de Graaf RA
authors.initials: R
authors.lastname: Kaptein
authors.initials: R
authors.lastname: Boelens