The conformation of the self-complementary decamer duplex, d(ACGTATACGT)2 (TATA-duplex) has been studied by proton NMR spectroscopy. The duplex is essentially B-type, with distortions apparent at the TATA steps. These conformational distortion which may be preferable to occur in the thymine residue on the 5'-side, has been investigated by unusual NOE crosspeaks.

The magnetic anisotropy effects of peptide group in structured protein on proton chemical shift have been investigated using trialanine modeling. The structure dependent part of chemical shift of C${\alpha}$H of the second amino acid residue was assumed to come purely from the magnetic anisotropy effects of C=O and C-N bonds of peptide in the direct neighborhood and thus to be dependent on and $\psi$ angle of this dipeptide. A set of dipeptide models with different and $\psi$angles were generated and from these models the chemical shift values were calculated using known algorithm to emphasize the role of parameters used in the equation. Comparison of sets of different parameters resulted in an optimized parameters which could reproduce the statistical chemical shift values observed in proteins with respect ot the secondary conformation.

The solution structure of bovine pancreatic trypsin inhibitor(BPTI) has been refined by NMR chemical shift data of C${\alpha}$H using classical molecular dynamics simulation. The structure dependent part of the observable chemical shift was modeled by ring current effect, magnetic anisotropy effect from the nearby groups, whereas the structure independent part was replaced with the random coil shift. A new harmonic function derived from the differences between the observed and calculated chemical shifts was added into physical force field as an pseudo potential energy term with force constant of 250 kJmol-1 ppm-2. During the 1.5 ns molecular dynamics simulation with chemical shift restraints BPTI has accessed different conformation space compared to crystal and NOE driven structure.

Deuterium quadrupole coupling constant (e2qzzQ/h) of ($\mu$3-C2H)[Co(CO)3]3 was determined by using solid-state deuterium MAS NMR spectroscopy. The small quadrupole coupling constant of bridging methyne unit relative to sp-acethylene in propyne is discussed in terms of the C-H bond length and the negative charge on the carbon.

Proper pulse sequences and experimental optimization for the 3D 15N edited TOCSY and NOESY spectra were described. Using sensitivity enhancement approach with coherent selection by pulsed field gradients described by Kay and co-workers, an considerable gain in sensitivity was achieved. The sensitivity was also improved by minimal water saturation using water flip-back pulse. Among the three types of TOCSY mixing pulse, named MLEV-17, DIPSI-2rc, DIPSI-2rc sequence gave the most sensitive spectrum. These results suggest an appropriate pulse sequence for for those 3D experiments for large proteins.

It has been demonstrated that mutant Hemoglobins (Hb) which have an altered ${\alpha}$1${\beta}$2 subunit interface can be designed. A compensatory mutation for a naturally occurring abnormal human Hb, Hb Kempsey (${\beta}$99Asp\longrightarrowAsn), has been designed, and this mutation allowed the molecule to regain its allosteric response. The calculated values for the difference in the free energy of cooperativity show excellent agreement with experimentally determined thermodynamic values, suggesting that the molecular dynamics simulation results can be used to obtain information about the specific interactions which contribute to the total free energy of cooperativity. These results provide encouragement to begin a systematic investigation of the molecular basis of the subunit interactions between the ${\alpha}$1 and ${\beta}$2 chains of Hb A by designing appropriate r Hbs. These studies could lead to the design of Hbs with desired cooperativity in the oxygenation process and to the restoration of functional properties of abnormal hemoglobins associated with hemoglobinopathies. Thus, the present results also have the implications in using gene therapy to treat patients with hemoglobinpathies.

Mesoporous MCM-41 gallosilicate material was synthesized through shifting through shifting gallosilicate polymer equilibrium towards a MCM-41 phase by addition of acid. The location of Cu(II) exchanged into MCM-41 and its interaction with various adsorbate molecules were investigated by electron spin responance and electron spin echo modulation spectroscopies. It was found that in the fresh hydrated material, Cu(II) is octahedrally coordinated to six water molecules. This species is located in a cylindrical channel and rotates rapidly at room temperature. Evacuation at room temperature removes three of these water molecules, leaving the Cu (II) coordinated to three water molecules and anchored to oxygens in the channel wall. Dehydration at 45$0^{\circ}C$ produces one Cu (II) species located in the inner surface of a channel as evidenced by broadening of its ESR lines by oxygen. Adsorption of polar molecules such as water, methanol and ammonia on dehydrated CuNa-MCM-41 gallosilicate material causes changes in the ESR spectrum of Cu (II), indicating the complex formation with these adsorbates. Cu (II) forms a complex with six molecules of methanol as evidenced by an isotropic room temperature ESR signal and ESEM data like upon water adsorption. Cu(II) also forms a complex containing four molecules of ammonia based on resolved nitrogen superhyperfine interaction.