$^{19}F$ NMR experiments were carried out to observe the change of the characteristics of the PVdF binder which is an auxiliary material of the lithium ion battery. PVdF has various crystalline or amorphous phases by thermal treatment. A mixture of cathode and auxiliary materials including PVdF was coated on aluminum foil as an electron collector and then subjected to thermal treatment at various temperatures. The overlapped $^{19}F$ NMR signals obtained from the various phases were separately convoluted into the respective phases, and it was found that there was a relative ratio change of these phases. In addition, the crystal and amorphous phase of PVdF was changed during the vacuum drying, which is the last step of the actual electrode manufacturing. It was observed that the relative amount of amorphous phase, which may affect the flexibility of the electrode or the wettability of the electrolyte, abruptly changes after a certain temperature.

Parahydrogen induced hyperpolarization (PHIP) technique is extensively studied to increase the sensitivity of the conventional NMR spectroscopy and recently try to apply this advanced technique into the revolutionary future of the MRI. The other hyperpolarization technique, which is widely utilized, is DNP (Dynamic Nuclear Polarization)-based hyperpolarization one. Despite its great advances in these fields, it contains several drawbacks to overcome: fast relaxation time, expensive equipment is needed, long build-up time is required (several hours), and batch scale material is hyperpolarized. To overcome all those limitations, one can effectively harness the hyperpolarized spin state of parahydrogen. One important step for utilizing the spin state of parahydrogen is doing well-developed experiments of ALTADENA and PASADENA. Based on those concepts, we successfully obtain the hydrogenation signals of ALTADENA and PASADENA from styrene by using benchtop NMR spectrometer. Also those signals were conceptually analyzed and confirmed with different mechanisms. To our best knowledge, those experiments using 1.4T (benchtop NMR) is the first reported one. Considering these experiments, we hope that parahydrogen-based hyperpolarization transfer studies in NMR/MRI will be broadened in Korea in the future.

A former study has shown that the spin-lattice relaxation time ($T_1$) in cancerous prostate tissue had enhanced contrast at an ultra-low magnetic field, $132{\mu}T$. To study the field dependence and the origin of the contrast we measured $T_1$ in pairs of ex-vivo prostate tissues at the Earth's magnetic field. A portable and coil-based nuclear magnetic resonance (NMR) system was adopted for $T_1$ measurements at $40{\mu}T$. The $T_1$ contrast, ${\delta}=1-T_1$ (more cancer)/$T_1$(less cancer), was calculated from each pair. Additionally, we performed pathological examinations such as Gleason's score, cell proliferation index, and micro-vessel density (MVD), to quantify correlations between the pathological parameters and $T_1$ of the cancerous prostate tissues.

The transcription factor CP2c has been recently validated as an oncogenic protein that can serve as a promising target for anticancer therapy. We have recently documented that a recombinant protein corresponding to the putative DNA-binding region (residues 63-244) of CP2c adopted two different conformers, one of which is dominated by zinc binding. However, in the present study, a longer construct encompassing residues 63-302 appeared to form a single structural domain. This domain could be considered to adopt a functionally relevant fold, as the known specific binding of a dodecapeptide to this protein was evident. Hence, the residues 63-302 region rather than 63-244 can be regarded as a natively folded structural domain of CP2c. In addition, it was confirmed that zinc ions can bind to this putative DNA-binding domain of CP2c, which resulted in reduced stability of the protein. In this context, it is suggested that the mode of action of CP2c would resemble that of tumor suppressor p53.

${\alpha}B$-crystallin (${\alpha}BC$) is a member of a small heat-shock protein (sHSP) superfamily and plays a predominant role in cellular protein homeostasis network by rescuing misfolded proteins from irreversible aggregation. ${\alpha}BC$ assembles into dynamic and polydisperse high molecular weight complexes containing 12 to 48 monomers; this variable stereochemistry of ${\alpha}BC$ has been linked to quaternary subunit exchange and its chaperone activity. The chaperone activity of ${\alpha}BC$ poses great potential as therapeutic agents for various neurodegenerative diseases. In this mini-review, we briefly outline the recent advancement in structural characterization of ${\alpha}BCs$ and its potential role to inhibit protein misfolding and aggregation in various human diseases. In particular, nuclear magnetic resonance (NMR) spectroscopy and its complimentary techniques have contributed much to elucidate highly-dynamic nature of ${\alpha}BCs$, among which notable advancements are discussed in detail. We highlight the importance of resolving the structural details of various ${\alpha}BC$ oligomers, their quaternary dynamics, and structural heterogeneity.

Studies on the interactions of proteins with partner molecules at the atomic resolution are essential for understanding the biological function of proteins in cells and for developing drug molecules. Solution NMR spectroscopy has shown remarkably useful capability for investigating properties on the weak to strong intermolecular interactions in both diluted and crowded solution such as cell lysates. Of note, the state-of-the-art in-cell NMR method has made it possible to obtain atomistic information on natures of intermolecular interactions between target proteins with partner molecules in living cells. In this mini-review, we comprehensively describe the several technological advances and developments in the in-cell NMR spectroscopy.