With the rapid increase of data on protein-protein interactions, the need for delineating the 3D structures of huge protein complexes has increased. The protocols for determining nuclear magnetic resonance (NMR) structure can be applied to modeling complex structures coupled with sparse experimental restraints. In this report, I suggest the use of multiple rigid bodies for improving the efficiency of NMR-assisted structure modeling of huge complexes using CYANA. By preparing a region of known structure as a new type of residue that has no torsion angle, one can facilitate the search of the conformational spaces. This method has a distinct advantage over the rigidification of a region with synthetic distance restraints, particularly for the calculation of huge molecules. I have demonstrated the idea with calculations of decaubiquitins that are linked via Lys6, Lys11, Lys27, Lys29, Lys33, Lys48, or Lys63, or head to tail. Here, the ubiquitin region consisting of residues 1-70 was treated as a rigid body with a new residue. The efficiency of the calculation was further demonstrated in Lys48-linked decaubiquitin with ambiguous distance restraints. The approach can be readily extended to either protein-protein complexes or large proteins consisting of several domains.

Resonance frequencies from the $^{113}Cd$ and $^{133}Cs$ nuclear magnetic resonance (NMR) spectra for the $CsCdBr_3$ single crystal were measured at varying temperatures by the static NMR method. The temperature-dependent changes of these frequencies are related to the changing structural geometry of the ${CdBr_6}^{4-}$ units, which affects the environment of $^{133}Cs$. The spin-lattice relaxation rates ($1/T_1$) for the $^{113}Cd$ and $^{133}Cs$ nuclei were measured in order to obtain detailed information about the dynamics of $CsCdBr_3$ crystals. The dominant relaxation mechanisms for $^{113}Cd$ and $^{133}Cs$ nuclei are direct single-phonon and Raman spin-phonon processes, respectively.

Nitrogen vacancy-centered diamond has recently emerged as a promising material for various applications due to its special optical and magnetic properties. In particular, its applications as a fluorescent biomarker with small toxicity, magnetic field and electric field sensors have been a topic of great interest. Recent review (R. Schirhagl et al 2014) introduced those applications using single NV-center in nanodiamond. In this minireview, I introduce the rapidly emerging DNP (Dynamic Nuclear Polarization) field using optically-pumped NV center in diamonds. Additionally, the possibility of exploiting the optically-pumped NV center for polarization transfer source, which will produce a profound impact on room temperature DNP, will be discussed.

Bean sprouts are often cultivated in the circumstances prevailing in the improper using of germicide and growth enhancer. The influence of ingestion those bean sprouts are unknown. The components of the bean sprouts are needed to evaluate for food safety. The extracts of the control, 0.5 g/L germicide, 1 g/L germicide, 12.5 mL/L growth enhancer and 25 mL/L growth enhancer were used to compare the components in the experiment. Nuclear Magnetic Resonance spectroscopy (NMR) was used to analyze the extracts. Statistical analysis of metabolomics showed significant changes between the control and head and the stem of the bean sprouts. Significant changes in metabolites were identified with the bean sprouts cultivated with germicide and growth enhancer by applying qualitative and quantitative analysis. Similar changes in the area of the bean sprouts were observed after treated to germicide and growth enhancer. Although treating germicide and growth enhancer showed no particular harmful metabolites changes to human, it made significant changes in the morphological and the metabolites of the bean sprouts. These changes indicate that the germicide and growth enhancer has substantially potential to influence the growth of the bean sprouts.

Transmembrane(TM) proteins are closely related to transport, channel formation, signaling, cell to cell interaction, so they are the crucial target of modern medicinal drugs. In order to study the structure and function of these TM proteins, it is important to prepare reasonable amounts of proteins. However, their preparation is seriously difficult and time-consuming due to insufficient yields and low solubility of TM proteins. We tried to produce large amounts of Syndecan-4 containing TM domain(SDC4-TM) that is related to the wound healing and tumor. Also, mutated SDC4-TM was studied to investigate structural change by modification of dimerization motif. We performed the structure determination by the Polarity Index at Slanted Angle (PISA) wheel pattern analysis based on $^{15}N-^1H$ 2D SAMPI-4 solid-state NMR of SDC4-TM and computational modeling using Discovery Studio 2016.

Replication Protein A (RPA) is the eukaryotic single-stranded DNA binding protein. It involves in DNA replication, repair, and damage response. Among three subunits, RPA70 has a protein-protein binding domain (RPA70N) at the N-terminal. It has known that the domain recruits several damage response proteins to the damaged site. Also, it is suggested that there are more candidates that interact with RPA70N. Even though several studies performed on the structural aspects of RPA70N and its ligand binding, the backbone assignments of RPA70N is not available in public. In this study, we present the backbone assignments of RPA70N.