• Analytical Science and Technology
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• v.17 no.5
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• pp.388-392
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• 2004

Structural studies of membrane proteins, importantly involving interpretation of genomics information, many signaling pathway and major drug target for drug discovery, are having difficulty in characterizing the function using conventional solution nmr spectroscopy and x-ray crystallography because phospholipid bilayers hindered fast tumbling and crystallization. Here, we studied the structure of the pf1 coat protein in oriented phospholipid bilayers by home-built solid-state NMR probe. Bacteriophage pf1 was purified from Paeudomonas Aeruginosa and coat protein of bacteriophage pf1 was isolated from DNA and other proteins.

• Bulletin of the Korean Chemical Society
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• v.31 no.5
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• pp.1187-1191
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• 2010

$^1H-^{15}N$ heteronuclear dipolar coupling solid-state NMR experiments on lipid bilayer or bicelle samples are very useful for the structural studies of membrane proteins. However, to study these biological samples using solid-state NMR, a specific probe with high efficiency and high capability is required. In this paper, we describe the optimized design, construction, and efficiency of a 400 MHz wide-bore $^1H-^{15}N$ solid-state NMR probe with 5-mm solenoidal rf coil for high power, multi-pulse sequence experiments, such as 2D PISEMA or 2D SAMMY.

• Bulletin of the Korean Chemical Society
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• v.34 no.3
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• pp.823-826
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• 2013

A low-${\varepsilon}$ solid-state NMR(Nuclear Magnetic Resonance) probe was developed for the spectroscopic analysis of two-dimensional $^{15}N-^1H$ heteronuclear dipolar coupling in dilute membrane proteins oriented in hydrated and dielectrically lossy lipid environments. The system employed a 800 MHz narrow-bore magnet. A solenoid coil strip shield was used to reduce deleterious RF sample heating by minimizing the conservative electric fields generated by the double-tuned resonator at high magnetic fields. The probe's design, construction, and performance in solid-state NMR experiments at high magnetic fields are described here. Such high-resolution solid-state NMR spectroscopic analysis of static oriented samples in hydrated phospholipid bilayers or bicelles could aid the structural analysis of dilute biological membrane proteins.

• Macromolecular Research
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• v.11 no.1
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• pp.53-61
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• 2003

A molecular-thermodynamic model is developed for the salt-induced protein precipitation. The protein molecules interact through four intermolecular potentials. An equation of state is derived based on the statistical mechanical perturbation theory with the modified Chiew's equation for the fluid phase, Young's equation for the solid phase as the reference system and a perturbation based on the protein-protein effective two body potential. The equation of state provides an expression for the chemical potential of the protein. In a single protein system, the phase separation is represented by fluid-fluid equilibria. The precipitation behaviors are simulated with the partition coefficient at various salt concentrations and degree of pre-aggregation effect for the protein particles. In a binary protein system, we regard the system as a fluid-solid phase equilibrium. At equilibrium, we compute the reduced osmotic pressure-composition diagram in the diverse protein size difference and salt concentrations.

• The Korean Journal of Food And Nutrition
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• v.11 no.6
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• pp.667-672
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• 1998

The possibility of solid-substrate fermentation of Lentinus edoes for the productin of protein-boud polysaccharides (PBP) was studied. Zeolite and orchid-pot soil were used as solid materials for the culture because of the desirable physical properties. Sucrose and starch were good carbon sources for the production of PBP by the solid-substrate fermentatin of L. edodes. Among the nitrogen source, bactosoyton was very effective for the PBP production. The optimum pH for solid-substrate fementation for the production of PBP was at pH of 5.5. The PBP production reached to 5∼5.5mg per 100g solid-substrate.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.3
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• pp.453-458
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• 1994

The nutrient content and protein quality of Giant snalil (Acchatina ) meats (white, yellow, and gray) were determined for fresh and processed products. Fresh snail meats contained 81~82% moisture, 11~14% protein, 0.9~1.3% fat, and 1.2-1.4% ash. Proximate composition of fresh meat varied (p<0.05) with meat colour and gray meat had the lowest protein and highest ash content among samples. The major minerals of fresh snail meats were calcium (318~570mg%), potassium (170~190mg%), and magnesium (74~103mg%).Gray meat showed the higher calcium and lower sodium level than the other snail meats. No differences were found between fresh snail meats on amino acid profile, and total essential amino acid was 46% of total amino acids in all snail meats. In vitro protein digestibility of fresh snail meats were ranged from 76 to 81% which were lower than that of marine moulusks. Processing resulted in some increase(1.7~5.7%) in protein digestibility but no differences were found in C-PER after processing. The 25% saline water extractable mucous materials from fresh snail meat influenced in decreasing digestibility of other protein sources from 2% (casein) to 11% (filefish protein).

• Journal of the Korean Magnetic Resonance Society
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• v.17 no.2
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• pp.81-85
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• 2013

Various fluorine-containing materials are used in electronic devices like LCD display panels and Li-ion batteries. The structural conformation of fluorine in fluorinated materials is an important contributing factor that influences the chemical and physical properties. The conformation can be changed by heat and stress during manufacture or use. Understanding the conformational changes is critical for understanding the performance and durability of electronic devices. Solid-state NMR spectroscopy could be widely used for the analysis of various fluorine-containing materials for electronic devices. However, conventional CPMAS probes cannot be used for in-situ analysis of fluorine-containing electronic devices like LCD panels and Li-ion batteries. In this paper, we show the design, construction, and optimization of a $^{19}F-^{13}C$ double-resonance solid-state NMR probe for a 400MHz wide-bore magnet with a flat square coil for in-situ analysis of fluorine-containing electronic devices without observing fluorine background signals. This custom-built probe does not show any fluorine background signals, and can have higher efficiency for lossy samples.

• Bulletin of the Korean Chemical Society
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• v.32 no.7
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• pp.2345-2350
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• 2011

Variable temperature high-resolution $^{19}F$ magic angle spinning (MAS) solid-state NMR spectroscopy was used to characterize fluorocarbon (FKM) rubbers. The high-resolution spectra of copolymers made from two monomers, vinylidene fluoride and hexafluoropropene, and terpolymers composed of vinylidene fluoride, hexafluoropropene, and tetrafluoroethylene, were obtained using MAS speeds of up to 18 kHz combined with high temperatures of up to 200 $^{\circ}C$ at a magnetic field strength of 9.4 Tesla. From these high resolution solid-state NMR spectra, we were able to assign the spectral peaks and differentiate the copolymer FKM from the terpolymer FKM. We also determined quantitatively the monomer compositions of each FKM rubber.

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.197-203
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• 2001

A fusion protein, consisting of human epidermal growth factor as a recognition domain and human angiogenin as a toxin domain, can be used as a targeted therapeutic against breast cancer cells among others. The fusion protein was expressed as inclusion body in recombinant E. coli, and when the conventional, solution-phase refolding process was used the refolding yield was very low due to severe aggregation, probably due to the opposite surface charge due to vastly different pI values of each domain. Solid-phase refolding process exploiting ionic interactions between the solid matrix and the protein was tried, but the ionic binding yield was very low regardless of the resins and pH conditions used. To provide higher affinity toward the solid matrix, six lysine residues were tagged to the N -terminus of the hEGF domain When the cation exchange resins such as heparin- or CM-Sepharose were used as the matrix, the adsorption capacity increased 2.5-3 times and the subsequent refolding yield increased nearly IS times compared to the conventional process.

• Biotechnology and Bioprocess Engineering:BBE
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• v.7 no.1
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• pp.1-5
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• 2002

A fusion protein, consisting of a human epidermal growth factor (hEGF) as the recognition domain and human angiogenin as the toxin domain, can be used as a targeted therapeutic against breast cancer cells among others. The fusion protein was expressed as inclusion body in recombinant E. coli, and when the conventional, solution-phase refolding process was used the refolding yield was very low due to severe aggregation. It was probably because of the opposite electric charge at a neutral pH resulting from the vastly different pI values of each domain. The solid-phase refolding process that exploited the ionic interactions between ionic exchanger surface and the fusion protein was tried, but the adsorption yield was also very low, below $ 30\%$, regardless of the resins and pH conditions used. Therefore, to provide a higher ionic affinity toward the solid matrix, six lysine residues were tagged to the N-terminus of the hEGF domain. When heparin-Sepharose was used as the matrix, the adsorption capacity increased 2.5-3 times to about $88\%$. Besides the intrinsic affinity of angiogenin to heparin, the poly-lysine tag provided additional ionic affinity. And the subsequent refolding yield increased nearly 13-fold, from ca. $4.8\%$ in the conventional refolding of the untagged fusion protein to $63.6\%$. The process was highly reproducible. The refolded protein in the column eluate retained RNase bioactivity of angiogenin.