HP1298 (Swiss-Prot ID ; P65108) is an 72-residue protein from Helicobacter pylori strain 26695. The function of HP1298 was identified as Translation initiation factor IF-l based on sequence homology, and HP1298 is included in IF-l family. Here, we report the sequence-specific backbone resonance assignments of HP1298. About 97% of all the $^{1}HN$, $^{15}N$, $^{13}C{\alpha}$, $^{13}C{\beta}$, and $^{13}CO$ resonances could be assigned unambiguously. We could predict the secondary structure of HP1298, by analyzing the deviation of the $^{13}C{\alpha}$ and $^{13}C{\beta}$ shemical shifts from their respective random coil values. Secondary structure prediction shows that HP1298 consists of six $\beta$-strands. This study is a prerequisite for determining the solution structure of HP1298 and investigating the structure-function relationship of HP1298. Assigned chemical shift can be used for the study on interaction between HP1298 and other Helicobacter pylori proteins.

The local structure of defects in undoped, Si-doped, and neutron irradiated free standing GaN bulk crystals, grown by hydride vapor phase epitaxy, has been investigated by employing electron magnetic resonance(EMR), Raman scattering and cathodoluminescence. The GaN samples were irradiated to a dose of $2{\times}10^{17}$ neutrons in an atomic reactor at Korea Atomic Energy Research Institute. There was no appreciable change in the Raman spectra for undoped GaN samples before and after neutron irradiation. However, a forbidden transition, $A_1$(TO) mode, appeared for a neutron irradiated Si-doped GaN crystal. Cathodoluminescence spectrum for the neutron irradiated Si-doped GaN crystal became much broader or was much more broadened than that for the unirradiated one. The observed EMR center with the g value of 1.952 in a neutron irradiated Si-doped GaN may be assigned to a Si-related complex donor.

Solid HETCOR (Hetero-Correlation) requires homo-dipolar decoupling between proton spins during the evolution and the mixing period in 2D-NMR. There are two different ways of achieving it with pulse sequences. One is based on the multiple pulse (MP) sequence where thousands of intense radio frequency (rf) pulses are used to remove the homo-dipolar interaction between protons. The other is utilizing the so-called Lee-Goldburg (LG) off-resonance scheme where a continuous rf-irradiation is used. In this report, the advantage of one technique to the other, is analyzed. LG version is evaluated better in S/N and easier in setup procedure with the same experimental time.

Function of protein is frequently related with tautomeric states of histidine sidechains. Thus, several NMR experiments were developed to determine the tautomeric states of histidines. However, poor sensitivity of these experiments caused by long duration of magnetization transfer periods is unavoidable. Here, we alleviate the sensitivity of HCN experiment for determining the tautomeric states of histidine residues using TROSY principle to suppress transverse relaxation of $^{13}C$ spins during long polarization transfer delays involving $^{13}C-^{15}N$ scalar couplings. In addition, this experiment was used to assign the sidechain resonances of histidines. These assignments can be used to follow the pH-titration of histidine sidechains.

Direct quantification of methanol in polymer electrolyte membrane (PEM) by solid-state nuclear magnetic resonance (NMR) spectroscopy was studied and the methanol concentrations in PEM produced by crossover and diffusion were compared. The error range of the quantification was not smaller than ${\pm}15%$ and the amount of the methanol crossed over in our direct methanol fuel cells (DMFCs) was less than the methanol diffused to PEM. The methanol concentration in the PEM of the DMFC operated at different current densities were equivalent.

Spin Hamiltonian for the paramagnetic center with a three-fold symmetry and high spin ($S{\geq}2$) multiplicity should contain the fourth order zero-field splitting (ZFS) terms. Electron magnetic resonance transition lines of the center with S = 5/2 are expected to split in a pair when the magnetic field is applied off the principal axes of ZFS, while they are superimposed when the magnetic field is applied parallel to the principal axes of ZFS. In this study we report that the transition lines of $Mn^{2+}$ centers at the three-fold symmetric sites in $LiNbO_3$, chemically equivalent but physically different, split in two due to the nonzero fourth order ZFS term.

The mechanism of charge flow has been probed by measuring the $^{1}H$ chemical shift on a proton-irradiated ${KH_2}{PO_4}$ (KDP) single crystal. The proton irradiation caused the increase in $^{1}H$ chemical shift. It can be interpreted as the electronic charge transfer from the proton to oxygen atom, accompanied with the proton displacement along the hydrogen bond. For the high resolution $^{1}H$ chemical shift measurement, CRAMPS (Combined Rotation And Multiple Pulses) technique is utilized.