An ion-exchanged reaction of $MnCl_2$ with Al-incorporated solid core/mesoporous shell silica (AlSCMS) followed by calcinations generated manganese species, where average oxidation state of manganese ion is 3+, in the mesoporous materials. Dehydration results in the formation of $Mn^{2+}$ ion species, which can be characterized by electron spin resonance (ESR). The chemical environments of the manganese centers in Mn-AlSCMS were investigated by diffuse reflectance, UV-VIS and ESR spectroscopic methods. Upon drying at 323 K, part of manganese is oxidized to higher oxidation state ($Mn^{3+}$ and $Mn^{4+}$) and further increase in (average) oxidation state takes place upon calcinations at 823 K. It was found that the manganese species on the wall of the Mn-AlSCMS were transformed to tetrahedral $Mn^{3+}$ or $Mn^{4+}$ and further changed to square pyramid by additional coordination to water molecules upon hydration. The oxidized $Mn^{3+}$ or $Mn^{4+}$ species on the surfaces were reversibly reduced to $Mn^{2+}$ or $Mn^{3+}$ species or lower valances by thermal process. Mn(II) species I with a well resolved sextet was observed in calcined, hydrated Mn-AlSCMS, while Mn (II) species II with g = 5.1 and 3.2 observed in dehydrated Mn-AlSCMS. Both species I and II are considered to be non-framework Mn(II).

The structural phase transition of $Cs_2MnCl_4{\cdot}2H_2O$ single crystals was investigated by determining the $^{133}Cs$ spin-lattice relaxation time $T_1$. The number of resonance lines in the $^{133}Cs$ spectrum changes from seven to one near 375 K, which means that above 375 K the Cs sites are symmetric. Further, the $T_1$ of the $^{133}Cs$ nucleus undergoes a significant change near 375 K, which coincides with the change in the splitting of the $^{133}Cs$ resonance lines. The change in $T_1$ near $T_C$ is related to the loss of $H_2O$, and means that the forms of the octahedra of water molecules surrounding $Cs^+$ are disrupted.

Human melanocortin-4 receptor (hMC4R) has a critical role in part of energy homeostasis, and their heterozygous mutations related in genetic cause of severe human obesity. In order to study the structure and function of these membrane proteins, it is important to prepare the samples. However, the preparation of transmembrane peptide is seriously difficult and time-consuming. Overexpression and purification of membrane proteins was reported to be difficult due to their innate insoluble and toxic properties. Among the many difficulties, the most important is the difficulty in obtaining sufficient quantities of purified protein. Recently, we succeed to produce large amounts of the second transmembrane domain from the wild-type hMC4R (wt-TM2) and D90N mutant hMC4R (m-TM2) and proposed the structural difference of them in membrane-like environments. In this paper, we demonstrate the optimization procedures to express and purify wt-TM2 or m-TM2 peptides, and solution NMR studies in different detergents to get high-resolution spectra were also described.

SH3YL1, a novel protein containing one Src homology 3 domain at the carboxyl terminus was first detected in mouse anagen skin cDNA. This protein had a significant homology with YHRO 16c/Ysc 84, the yeast Src homology 3 domain-containing protein. The sequence identity was remarkable at the carboxyl and amino-terminal Src homology 3 domain, suggesting that the novel protein is a mouse homolog of the yeast protein and thus was termed as SH3YL1. SH3YL1 is composed of two domains, a DUF500 at N-termini and a SH3 domain at C-termini. In our study we cloned the SH3 domain in bacterial expression system in Escherichia coli using pET32a vector with TEV protease cleavage site and purified as a monomer using affinity chromatography. The N-terminal poly-Histidine tag was cleaved with TEV protease and target protein was used for backbone studies. Our study showed that SH3 domain primarily consists of $\beta$-sheet which is in consistence with previous result performed on the truncated SH3 domain of SH3YL1.

Hsp33 is a molecular chaperone achieving a holdase activity upon response to a dual stress by heat and oxidation. Despite several crystal structures available, the activation process is not clearly understood, because the structure inactive Hsp33 as its reduced, zinc-bound, monomeric form has not been solved yet. Thus, we initiated structural investigation of the reduced Hsp33 monomer by NMR. In this study, to overcome the high molecular weight (33 kDa), the protein was triply isotope-[$^{13}C$, $^{15}N$, $^2H$]-labeled and its inactive, monomeric state was ensured. 2D-[$^1H$, $^{15}N$]-TROSY and a series of triple resonance spectra could be successfully obtained on a high-field (900 MHz) NMR machine with a cryoprobe. However, under all of the different conditions tested, the number of resonances observed was significantly less than that expected from the amino acid sequence. Thus, a possible contribution of dynamic conformational exchange leading to a line broadening is suggested that might be important for activation process of Hsp33.

Redox-dependent conformational change of human 8-kDa Dynein light chain (LC8) plays important role in regulating NF-${\kappa}B$ signaling pathway. In this study we characterized the structural states of the oxidized and reduced forms of LC8 by using NMR spectroscopy. The $^1H-^{15}N$ 2D HSQC spectra of oxidized LC8 indicated that no significant change in tertiary structure of LC8 occurred upon oxidation. The chemical shift perturbations of LC8 upon oxidation suggest a redox-dependent quaternary structural change.

We studied the hydrogen-bonded $TlH_2PO_4$ (TDP) ferroelectrics treated with the proton-beam bombardment. The TDP material was irradiated with 1-MeV proton beam at a dose of $10^{15}/cm^2$. In order to analyze the hydrogen environment in TDP, we carried out the $^1H$ high resolution nuclear magnetic resonance (NMR) - i.e., Combined Rotation And Multiple Pulse Spectroscopy (CRAMPS) measurement. The isotropic chemical shift of hydrogen indicates its displacive property is related to the $PO_4$ lattice deformation which occurs throughout the antiferroelectric-, the ferroelastic- and the paraelastic-phase transitions. The temperature dependence of $\sigma_{iso}$ reveals the electronic charge redistribution is induced by the proton-beam irradiation and the elastic property.

Conformational properties of several mono-alkyl ester derivatives of p-tert-butylcalix[6]arene depending on temperatures have been investigated by solution NMR spectroscopy. It is found out that all derivatives can adopt a cone-like conformation around room temperature, while the conformational characteristics at high temperatures seem to be quite different each other.