Coffee is one of the top selling products in the world. There are various coffee bean species around the world. Among them, Coffea Arabica is the most popular species. However, there are few studies on the metabolites of coffee beans so far. This study demonstrates effects of the planted regions on the metabolite concentrations of coffee beans. The metabolites of coffee beans can be affected by growing area even although same species are grown. Accordingly, we studied coffee bean metabolites extracted from the same species in different regions (The brand names, Kona from Hawaii, Mocha Matari from Yemen, and Blue Mountain from Jamaica) by using mixed solvent of methanol: water: chloroform. A comparative analysis by NMR spectroscopy was performed and the statistical techniques were used to figure out the differences. As a result, we found that chlorogenic acid, caffeine, citrate, and sucrose mainly contributed to the separation of the three groups. When compared with Kona and Blue Mountain, concentrations of chlorogenic acid, caffeine, and sucrose in Mocha Matari were observed to be relatively down-regulated. In addition, compared with the two other groups, concentration of citrate in Kona was observed to be up-regulated.

Cupin-superfamily proteins represent the most functionally diverse groups of proteins and include a huge number of functionally uncharacterized proteins. Recently, YaiE, a cupin protein from Escherichia coli has been suggested to be involved in a novel activity of pyrimidine/purine nucleoside phosphorylase (PPNP). In the present study, we achieved a complete backbone NMR assignments of YaiE, by a series of heteronuclear multidimensional NMR experiments on its [$^{13}C/^{15}N$]-enriched sample. Subsequently, secondary structure analysis using the assigned chemical shift values identified 10 obvious ${\beta}-strands$ and a tentative $3_{10}-helix$. Taken all together, the results constitute the first structural characterization of a putative PPNP cupin protein.

It is now well established that RNAs exhibit fundamental roles in regulating cellular processes. Many of these RNAs do not exist in a single conformation. Rather, they undergo dynamic transitions among many different conformations to mediate critical interactions with other biomolecules such as proteins, RNAs, DNAs, or small molecules. Here, we briefly review NMR techniques that describe the dynamic behavior of RNA by determining structural, kinetic, and thermodynamic properties.

The $^{14}N$ NMR spectra for $(NH_4)_2SO_4$ crystals were obtained near the phase transition temperature $T_C=223K$, and were found to precisely reflect the symmetry change in the crystal at this first-order phase transition. Changes in the resonance frequencies near $T_C$ were attributed to the structural phase transition. In the ferroelectric and paraelectric phases, two inequivalent NH4 groups were distinguished in the $^{14}N$ NMR spectra. The two types, $NH_4$(1) and $NH_4$(2), have slightly different local environments. Consequently, we conclude that the phase transition is caused by the change in the environment of the $^{14}N$ nuclei in the $NH_4$ groups, rather than by the $SO_4$ groups.

At high temperature, the roles of $NH_4$ and $H_2O$ in $(NH_4)_2Fe(SO_4)_2{\cdot}6H_2O$ and $(NH_4)_2Zn(SO_4)_2{\cdot}6H_2O$ single crystals were investigated using a pulse NMR spectrometer. Temperature was shown to have a significant influence, causing changes in the deformation of $NH_4$ and $H_2O$. From the $^1H$ NMR and $^{14}N$ NMR spectrum, the forms of environment surrounding $^{14}N$ in $NH_4$ groups is more important than the loss of $H_2O$ groups. NMR studies indicate that $NH_4{^+}$ ions in Tutton salts play an important role in the changes of the crystal structure at high temperatures.

${\beta}-catenin$ is a key signaling protein which regulates cell signaling and gene transcription. Abnormal activation of ${\beta}-catenin$ is linked to many cancers, particularly with colorectal cancers. Although many genetic and biological studies on $Wnt/{\beta}-catenin$ have been reported and structures of the complex between ${\beta}-catenin$ and its diverse binding partners have been published, many of them have focused on armadillo repeat domain of ${\beta}-catenin$. Both N- and C-terminal domains have been suggested to regulate interactions of ${\beta}-catenin$ with other molecules, but still little is known about the C-terminal unstructured domain. To investigate the structure of this domain, construct of C-terminus was designed and structural studies were performed using size exclusion chromatography (SEC), circular dichroism (CD), fluorescence and nuclear magnetic resonance (NMR) spectroscopy. We observed that not only the purified full-length construct but the purified C-terminal construct also dimerizes in solution by SEC, suggesting that this domain involves in dimerization of ${\beta}-catenin$. CD and fluorescence data indicate its flexibility and structural formation in the presence of membrane environments.