PRACTICAL ASPECTS OF 2-DIMENSIONAL PROTON-DETECTED N-15 SPIN RELAXATION MEASUREMENTS

An investigation has been made into several aspects of the acquisition and processing of NMR data used to obtain heteronuclear relaxation parameters in proteins. Pulse sequences are described that reduce the time required to acquire relaxation data by a factor of two without sacrificing precision or accuracy of the results. In addition, a number of factors that influence the accuracy and precision of measured relaxation parameters, including uncertainties in peak intensities, overlap between resonances, and amide-proton exchange with solvent, are examined theoretically and experimentally. The results provide guidelines for maximizing the reliability of investigations of spin relaxation in proteins. © 1993 Academic Press, Inc.