High-resolution three-dimensional solid-state NMR spectroscopy of a uniformly 15N-labeled protein Academic Article uri icon

abstract

  • Since the earliest days of protein NMR spectroscopy, isotopic labeling strategies', 2 have been at least as important as instrumentation and spectroscopic methods in contributing to the success of experimental investigations. Significant progress in these three areas has made NMR spectroscopy a generally applicable method for the determination of the structures of globular proteins in s~ lution.~ Additional developments are needed so that solid-state NMR spectroscopy can extend the range of proteins whose structures can be determined to include those in membranes and other supramolecular structures. Uniform I5N labeling of proteins, which can be readily and inexpensively accomplished by expression in bacteria grown on a medium with I5NH4Cl as the sole nitrogen source," was originally implemented for solid-state5 and then extended to solution6 NMR because of …

publication date

  • January 1, 1995