Nuclear magnetic resonance (NMR) spectroscopy, extensively and successfully employed in many fields, has become one of the most important tools for studying biological macromolecules with the remarkable progress in both experimental techniques and hardware improvement in the past decades. This article briefly introduces recent significant progress in experimental techniques capable of improving sensitivity and resolution of spectra for very large biomolecules (> 50 kDa) and refinement of protein structures. In addition, conventional experiments of multidimensional NMR are very time-consuming to achieve well-resolved spectra. Recent advance of experiment techniques for shortening days-long acquisition time is also mentioned.
Nuclear magnetic resonance (NMR) spectroscopy, extensively and successfully employed in many fields, has become one of the most important tools for studying biological macromolecules with the remarkable progress in both experimental techniques and hardware improvement in the past decades. This article briefly introduces recent significant progress in experimental techniques capable of improving sensitivity and resolution of spectra for very large biomolecules (> 50 kDa) and refinement of protein structures. In addition, conventional experiments of multidimensional NMR are very time-consuming to achieve well-resolved spectra. Recent advance of experiment techniques for shortening days-long acquisition time is also mentioned.