• Journal of the Korean Chemical Society
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• v.29 no.5
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• pp.533-538
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• 1985

To investigate the importance of the hydrophobic interaction in the spermine-induced collapse of DNA to a compact structure, the effect of urea on the anomalous absorbance-temperature profile of calf thymus DNA has been investigated. With the increase of the urea concentration, the trough phase of the anomalous absorbance-temperature profile was eliminated eventually. The cooperativity, enthalpy, and the midpoint of the transition to the trough region are more sensitive to urea than those of the Tm-region transition. The present data of the adverse effect of urea, a hydrophobic environmental reagent, on the thermal stabilization of the condensed state of DNA, suggest that hydrophobic interaction may play an important role in the stabilization of the tertiary structure of the collapsed state of DNA.

• Journal of the Korean Chemical Society
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• v.63 no.6
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• pp.427-434
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• 2019

The role of hydrophobic residues on protein folding reaction was studied by folding kinetics measurements in conjunction with protein engineering. The HubWA, which was derived from human ubiquitin by mutating the residues at 45 (Phe to Trp) and 26 (Val to Ala), was used as a mutational background. Fourteen hydrophobic residues were mutated to alanine. Among fourteen variants generated, only four variant proteins (V5A, I13A, V17A, and I36A) were suitable for folding study. The folding kinetics of these variants was measured by stopped-flow fluorescence spectroscopy. The folding kinetics of HubWA and V17A was observed to follow a three-state on-pathway mechanism. On the other hand, folding kinetics of V5A, I13A, and I36A was observed to follow a two-state mechanism. Based on these observations, transition of protein folding reaction from collision-diffusion mechanism to nucleation-condensation mechanism was discussed.

• Restorative Dentistry and Endodontics
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• v.34 no.1
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• pp.42-50
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• 2009

Deterioration of long-term dentin adhesion durability is thought to occur by hydrolytic degradation within hydrophilic domains of the adhesive and hybrid layers. This study investigated the hypothesis that priming the collagen network with an organic solvent displace water without collapse and thereby obtain good bond strength with an adhesive made of hydrophobic monomers and organic solvents. Three experimental adhesives were prepared by dissolving two hydrophobic monomers, bisphenol-A-glycidylmethacrylate (Bis-GMA) and triethyleneglycol dimethacrylate (TEGDMA), into acetone, ethanol or methanol. After an etching and rinsing procedure, the adhesives were applied onto either wet dentin surfaces (wet bonding) or dentin surfaces primed with the same solvent (solvent-primed bonding). Microtensile bond strength (MTBS) was measured at 48 hrs, 1 month and after 10,000 times of thermocycles. The bonded interfaces were evaluated using a scanning electron microscope (SEM). Regardless of bonding protocols, well-developed hybrid layers were observed at the bonded interface in most specimens. The highest mean MTBS was observed in the adhesive containing ethanol at 48 hrs. With solvent-primed bonding, increased MTBS tendencies were seen with thermo cycling in the adhesives containing ethanol or methanol. However, in the case of wet bonding, no increase in MTBS was observed with aging.