• Journal of the Korean Chemical Society
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• v.19 no.1
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• pp.21-33
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• 1975

cis-and trans-2-butenedialdioximes are synthesized via 2-butenedials, very unstable precursors, and the conformation of the cis-isomer of those compounds is determined by the NMR spectra of 1,4-dideutero-and 1-deutero-cis-2-butenedialdioximes; it is certain that the conformation has an unsymmetrical structure as shown below.

• Journal of Integrative Natural Science
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• v.7 no.2
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• pp.79-86
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• 2014

Amyloid oligomers are believed to play important causal roles in many types of amyloid-related degenerative diseases. Many different laboratories have reported amyloid oligomers that differ in size, morphology, toxicity, and method of preparation or purification, raising the question of the structural relationships among these oligomer preparations. The structural plasticity that has been reported to occur in amyloid formed from the same protein sequence indicates that it is quite possible that different oligomer preparations may represent distinct structural variants. In view of the difficulty in determining the precise structure of amyloids, conformation- and epitope-specific antibodies may provide a facile means of classifying amyloid oligomer structures. Conformation-dependent antibodies that recognize generic epitopes that are specifically associated with distinct aggregation states of many different amyloid-forming sequences indicate that there are at least two fundamentally distinct types of amyloid oligomers: fibrillar and prefibrillar oligomers. Classification of amyloid oligomers according to their underlying structures may be a more useful and rational approach than relying on differences in size and morphology.

• International Journal of Advanced Culture Technology
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• v.11 no.2
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• pp.323-329
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• 2023

In this study, Proline pentamer model was used to investigate change in the dihedral angle, intramolecular hydrogen bonding and formation energies during structural optimization. L-Proline (LP, as an imino acid residue) pentamers having four conformation types [β: φ/ψ=t−/t+, α: φ/ψ=g−/g−, PP_II: φ/ψ=g−/t+ and Plike: φ/ψ= g−/g+] were carried out by QCC [B3LYP/6-31G(d,p)]. The optimized structure and formation energy were examined for designated structure. In LP, P-like and PP_II types did not change by optimization, and β types were transformed into PP_II having no H-bond independently of the designated ψ values. PP_II was more stable than P-like by about 2.2 kcal/mol/mu. The hydrogen bond distances of d2(4-6) type H-bonds were 1.94 - 2.00Å. In order to understand the processes of the transformations, the changes of φ/ψ, distances of NH-OC (d_NH/CO) and formation energies (ΔE, kcal/mol/mu) were examined.

• Bulletin of the Korean Chemical Society
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• v.32 no.10
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• pp.3702-3706
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• 2011

The conformation of a neuropeptide, substance P (SP), in isotropic (q = 0.5) acidic bicelles was investigated using two-dimensional NMR techniques. By the nuclear Overhauser effect (NOE) cross peaks between SP and long-chain lipid molecules SP was probed to bind on the flat surface of the disc-like bicelles. Structural analysis of NMR data indicated that the helical conformation of SP extended to the C-terminal region of Leu10 as well as in the mid-region from Pro4 to Phe8. As compared with the conformations of SP bound on the sodium dodecylsulfate (SDS) or the dodecylphosphocholine (DPC) micelles with curved surfaces, the surface curvature of the membrane mimics was found to be one of the major factors inducing the biologically relevant conformation of SP. The negative surface charge of the membrane is also a key factor inducing both the binding of SP on the membrane and its biologically active structure.

• Bulletin of the Korean Chemical Society
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• v.18 no.10
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• pp.1047-1050
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• 1997

• Korean Journal of Food Science and Technology
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• v.25 no.3
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• pp.277-281
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• 1993

To elucidate the conformational stability of proteins in colloidal food system, molecular properties of various proteins such as chemically modified ${\beta}-lactoglobulin$, bovine serum albumin (BSA) structural intermediates, and ${\beta}-casein$ under chaotropic conditions, were examined using circular dichroism, SS bond content, and hydrodynamic radius determination. As refolding time increases, BSA intermediates approach the conformation of native BSA. And succinylation made ${\beta}-lactoglobulin$ have more aperiodic structure by increasing net negative charge. Also, under chaotropic conditions, the conformation of P-casein was affected by hydrophobic interactions. This study clearly indicates that hydrophobic interactions and electrostatic interactions are major contributing factors in conformational stability of proteins.

• Journal of Sericultural and Entomological Science
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• v.45 no.2
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• pp.121-125
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• 2003

Dissolution of Antheraea pernyi silk fiber was carried out in a zinc nitrate 6 hydrate (Zn(NO$_3$)$_2$ㆍ6$H_2O$) solution with various dissolving conditions. The solubility was significantly dependent on the concentration of zinc nitrate, dissolving temperature and time. Regenerated A. pernyi silk fibroin powder was obtained through dialysis process to remove chaotropic salt. FTIR and X-ray diffractometer showed that the conformation of regenerated A. pernyi silk powder was sheet structure.

• Journal of Sericultural and Entomological Science
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• v.42 no.1
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• pp.42-47
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• 2000

Structural and thermal characteristics of silk fibroin/poly(2-hydroxyethyl methacrylate)(PHEMA) blend films were investigated using FTIR, X-ray diffractometer, differential scanning calorimeter, thermogravimeter and scanning electron microscope. FTIR spectra showed that the conformation of silk fibroin prepared by dissolving in formic acid was $\beta$-sheet, which did not affected by blending with PHEMA. The X-ray diffraction patterns also showed that individual crystalline structure of silk fibroin and PHEMA was not affected for the blend films. The initial thermal decomposition temperature of silk fibroin/PHEMA blend film tends to be higher than either of silk fkbroin or PHEMA. Thermal stability of both polymers, more notably PHEMA, can be improved by blending two components. As a result of SEM observation, the phases separation for silk fibroin/PHEMA blend films occured regardless of blend ratio ; continuous and dispersed phase were silk fibroin and PHEMA component, respectively.

• Applied Chemistry for Engineering
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• v.33 no.4
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• pp.425-430
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• 2022

L-alanine (LA, as an amino acid residue) pentamer model was used to investigate changes in the dihedral angle, intramolecular hydrogen bonding and formation energies during structural optimization. LA pentamers having four conformation types [𝛽: 𝜑/𝜓=t-/t+, 𝛼: 𝜑/𝜓=g-/g-, PP_II: 𝜑/𝜓=g-/t+ and P-like: 𝜑/𝜓= g-/g+] were carried out by quantum chemical calculations (QCC) [B3LYP/6-31G(d,p)]. In LA, 𝛽, 𝛼, and P-like types did not change by optimization, having an intra-molecular hydrogen bond: NH⋯OC (H-bond), and PP_II types in the absence of H-bond were transformed into P-like at the designated 𝜓 of 140°, and to 𝛽 at that of 160° or 175°. P-like and 𝛼 were about 0.5 kcal/mol/mu more stable than 𝛽. In order to understand the processes of the transformations, the changes of 𝜑/𝜓, distances of NH-OC (d_NH/CO) and formation energies (𝜟E, kcal/mol/mu) were examined.

• Molecules and Cells
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• v.25 no.3
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• pp.352-357
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• 2008

Osteoprotegerin (OPG) is a soluble decoy receptor that inhibits osteoclastogenesis and is closely associated with bone resorption processes. We have designed and determined the solution structures of potent OPG analogue peptides, derived from sequences of the cysteine-rich domain of OPG. The inhibitory effects of the peptides on osteoclastogenesis are dose-dependent ($10^{-6}M-10^{-4}M$), and the activity of the linear peptide at $10^{-4}M$ is ten-fold higher than that of the cyclic OPG peptide. Both linear and cyclic peptides have a ${\beta}$-turn-like conformation and the cyclic peptide has a rigid conformation, suggesting that structural flexibility is an important factor for receptor binding. Based on structural and biochemical information about RANKL and the OPG peptides, we suggest that complex formation between the peptide and RANKL is mediated by both hydrophobic and hydrogen bonding interactions. These results provide structural insights that should aid in the design of peptidyl-mimetic inhibitors for treating metabolic bone diseases caused by abnormal osteoclast recruitment.