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One way to overcome the intrinsically low sensitivity of Nuclear Magnetic Resonance spectroscopy is to enhance the signal by dynamic nuclear polarization (DNP), where the polarization of high-gyromagnetic ratio (γ) electrons is transferred to the surrounding nuclei using microwave (MW) irradiation. Recent developments in DNP instrumentations and applications have shown that DNP is one of the most effective methods to increase the nuclear spin polarization in inorganic, organic, and biological materials. It is possible to obtain a solution of molecules containing hyperpolarized nuclei in combination with methods to dissolve rapidly the polarized solid sample. In this chapter, a brief introduction on a theoretical basis and some of new DNP applications in NMR spectroscopy as well as medical applications in Magnetic Resonance Imaging (MRI) are described.

We report the full resonance assignments of MOD, which is an active mutant of maize ribosome-inactivating protein (mRIP). mRIP is a unique RIP which is synthesized as an inactive precursor and processed by removal of an internal inactivation region to yield an active form.

The described TROSY-based experiments for investigating backbone dynamics of proteins make it possible to elucidate internal motions in large proteins via measurements of T(1), T(2), and NOE of backbone (15)N nuclei. In our proposed sequences, the INEPT sequence is eliminated and the PEP sequence is replaced by the ST2-PT sequence from the HSQC-based experiments. This has the benefit of shortening the pulse sequences by 5.4 ms (=1/2J) and results in an increase in the intrinsic sensitivity of the proposed TROSY-based experiments. The TROSY-based experiments are on average of 13% more sensitive than the corresponding HSQC-based experiments on a uniformly (15)N-labeled Xenopus laevis calcium-bound calmodulin sample on a 750-MHz spectrometer at 5 degrees C. The amide proton linewidths of the TROSY-based experiments are 2-13 Hz narrower than those of the HSQC experiments. More sensitivity gain and higher resolution are expected if the protein sample is deuterated., (Copyright 2000 Academic Press.)