Among several NMR hyperpolarization techniques, parahydrogen-based hyperpolarization technique is recently extensively utilized to enhance the sensitivity of the conventional NMR/MRI spectroscopy. Two mostly investigated research topics are PHIP (Parahydrogen Induced Polarization) and SABRE (Signal Amplification By Reversible Exchange), which are commonly using the parahydrogen as the source of hyperpolarization. Those researches have been considered as the promising techniques that could provide hyperpolarized states on the ambient substrates including biologically important materials. Therefore, based on their potentials, we briefly reviewed several important experimental results on those topics after introducing the basic principle of parahydrogen and its generation with conceptual explanations. We hope this review will broaden the parahydrogen-based hyperpolarization transfer study on many researches in Korea.

Metabolite identification and quantification are one of the foremost important issues in metabolomics. In NMR based metabolomics, mainly one-dimensional proton NMR spectra of biofluids, such as urine and serum are measured. However, it is not always easy to identify and quantify metabolites in one-dimensional proton NMR spectra. This article introduces useful public metabolite databases, metabolic profiling software, and articles.

Replication protein A (RPA) is an essential single-stranded DNA binding protein in DNA processing. It is known that N terminal domain of RPA70 (RPA70N) recruits various protein partners including damage-response proteins such as p53, ATRIP, Rad9, and MRE11. Although the common binding residues of RPA70N were revealed, dynamic properties of the protein are not studied yet. In this study, we measured $^{15}N$ relaxation parameters ($T_1,\;T_2$ and heteronuclear NOE) of human RPA70N and analyzed them using model-free analysis. Our data showed that the two loops near the binding site experience fast time scale motion while the binding site does not. It suggests that the protein binding surface of RPA70N is mostly rigid for minimizing entropy cost of binding and the loops can experience conformational changes.