• Journal of Photoscience
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• v.9 no.2
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• pp.114-117
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• 2002

Ultraviolet resonance Raman (UVRR) spectroscopy was used to elucidate the dynamic change of the protein structure of bacteriorhodopsin (BR) during the photocycle. The photointermediates minus light- adapted (LA) BR difference spectra show Trp difference signals, which are assigned to Trp189 or Trp182 on helix F by using the mutants, W182F and W189F. The Difference signals of Trp 182 indicates an increase in hydrogen bonding strength at the indole nitrogen and a large change in the side chain conformation (X$\^$2,1/ torsion angle) in the M$_1$ \longrightarrow M$_2$ transition. On the other hand, Trp189 shows an increased hydrophobic interaction. These results suggest that the tilt of helix F occurs in the M$_1$\longrightarrow M$_2$ transition. In the M$_2$ \longrightarrow N transition, the hydrophobic interaction of Trp182 decreases drastically, The decrease in hydrophobic interaction of Trp182 in the N state suggests an invasion of water molecules that promote the proton transfer from Asp96 to the Schiff base. Structural reorganization of the protein after the tilt of helix F may be important for efficient reprotonation of the Schiff base.

• Journal of Nutrition and Health
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• v.30 no.6
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• pp.658-668
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• 1997

Path of a small hydrophobic molecule through the aqueous cytoplasma is not linear. Partition may favor membrane binding by several orders of magnitude : thus significant membrane association will markedly decrease the cytosolic transport rate. The presence of high concentration of soluble binding proteins for these hydrophobic molecules would compete with membrane association and thereby increase transport rate. For long chain fatty acid molecules, a family of cytosolic binding proteins collectively known as the fatty acid binding proteins(FABP), are thought to act as intracellular transport proteins. This paper examines the mechanism of transfer of fluorescent antyroyloxy-labeled fatty acids(AOFA) from purified FABPs to phosholipid membranes. With the exception of the liver FABP, AOFA is transferred from FABP by collisional interaction of the protein with a acceptor membrane. The rate of transfer increased markedly when membranes contain anionic phospholipids. This suggests that positively charged residues on the surface of the FABP may interact with the membranes. Neutralization of the surface lysine residues of adipocyte FABP decreased fatty acid transfer rate, and transfer was found to proceed via aqueous diffusion rather than collisional interaction. Site specific mutagenesis has further shown that the helix-turn-helix domain of the FABP is critical for interaction with anionic acceptor membranes. Thus cytosolic FABP may function in intracellular transport of fatty acid to decrease their membranes association as well as to target fatty acid to specific subcellular sites of utilization.

• Microbiology and Biotechnology Letters
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• v.17 no.3
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• pp.219-223
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• 1989

Effect of antifoam agents, silicone oil and neolin 302, was investigated on the production of prodnisolone by microbial $\Delta$$^1$-Dehydrogenation of hydrocortisone. The microbial process was conduct-ed by using a pseudo-crystallofermentation. By the hydrophobic-hydrophobic interaction, the steroid crystals aggregated with the antifoam agents. The aggregation resulted in a decrease of total mass transter area of substrate particles which is proportional to the dissolution rate of the solid substrate, and it consequently led to a significant decrease of the bioconversion rate. The bioconversion with neolin proceeded more slowly than with silicone oil. Increase of the concentration of the antifoam agents also yielded a significant decrease of the bioconversion rate.

• Bulletin of the Korean Chemical Society
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• v.6 no.1
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• pp.23-29
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• 1985

The charge-transfer complexing properties of 1-methyl nicotinamide (MNA), an acceptor, and adenine, a donor, were investigated in water and SDS micellar solutions in relation to the intramolecular interaction in nicotinamide adenine dinucleotide ($NAD^+$). The spectral and thermodynamic parameters of MNA-indole and methyl viologen-adenine complex formations were determined, and the data were utilized to evaluate the charge-transfer abilities of MNA and adenine. The electron affinity of nicotinamide was estimated to be 0.28 eV from charge-transfer energy $of{\sim}300$ nm for MNA-indole. The large enhancement of MNA-indole complexation in SDS solutions by entropy effect was attributed to hydrophobic nature of indole. The complex between adenine and methyl viologen showed an absorption band peaked near 360 nm. The ionization potential of adenine was evaluated to be 8.28 eV from this. The much smaller enhancement of charge-transfer interaction involving adenine than that of indole in SDS solutions was attributed to weaker hydrophobic nature of the donor. The charge-transfer energy of 4.41 eV (280 nm) was estimated for nicotinamide-adenine complex. The spectral behaviors of $NAD^+$ were accounted to the presence of intramolecular interaction in $NAD^+$, which is only slightly enhanced in SDS solutions. The replacement of nicotinamide-adenine interaction in $NAD^+$ by intermolecular nicotinamide-indole interaction in enzyme bound $NAD^+$, and guiding role of adenine moiety in $NAD^+$ were discussed.

• Bulletin of the Korean Chemical Society
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• v.34 no.3
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• pp.743-748
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• 2013

The temperature dependence of the partition coefficients of a neuropeptide, substance P (SP), in isotropic acidic bicelles was investigated by using a pulsed field gradient nuclear magnetic resonance diffusion technique. The addition of negatively charged dimyristoylphosphatidylserine to the neutral bicelle changed the SP partitioning a little, which implies that the hydrophobic interaction between the hydrophobic residues of SP and the acyl chains of lipid molecules is the major interaction while the electrostatic interaction is minor in SP binding in a lipid membrane. From the temperature dependence of the partition coefficients, thermodynamic functions were calculated. The partitioning of SP into the acidic bicelles is enthalpy-driven, as it is for small unilamellar vesicles and dodecylphosphocholine micelles, while peptide partitioning into a large unilamellar vesicle is entropy-driven. This may mean that the size of lipid membranes is a more important factor for peptide binding than the surface curvature and surface charge density.

• Membrane Journal
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• v.31 no.2
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• pp.145-152
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• 2021

While there are increasing demands on biomolecules separation, resin chromatography lacks in terms of throughput and membrane chromatography is an alternative with high binding capacity and enhanced mass transfer properties. Unlike typical membrane processing, where the performance can only be empirically assessed, understanding how mechanisms work in membrane chromatography is decisive to design biospecific processing. This short review covers three separation mechanisms, including affinity interaction modes for selectively capturing bulk molecules using biospecific sites, ion exchange modes for binding biomolecules using net charges and hydrophobic interaction modes for binding targeted, hydrophobic species. The parameters in designing membrane chromatography that should be considered operation-wise or material-wise, are also further detailed in this paper.

• Journal of the Korean Chemical Society
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• v.39 no.8
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• pp.666-671
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• 1995

The conformational properties of poly(ethylene oxide) (PEO) in aqueous solutions are studied by viscometry with respect to the water structure perturbing capabilities of a series of urea solutes at $16^{\circ}C$, and experiments for the effect of amounts of urea and methylurea on PEO at 16 and $25^{\circ}C$ are also performed. The results show that the chain expansion, by ureas, of PEO of $1.0{\times}10^5$ molecular weight at $16^{\circ}C$ is similar to that of PEO of $8.0{\times}10^3$ molecular weight at $25^{\circ}C$ with respect to the water structure perturbation. Urea and methylurea make the PEO chain expand by the perturbation of water structure around PEO and by the hydrophobic interaction between methylurea and PEO, respectively. PEO of $1.0{\times}10^5$ molecular weight has hydrophobic sites on it, which are roughly classified into two parts; one is the inner hydrophobic groups which can interact between themselves (intramolecular hydrophobic interaction) and prevails at $16^{\circ}C$, and the other is the outer, exposed hydrophobic groups which can interact with the added hydrophobic solute (intermolecular hydrophobic interaction) and prevails at $25^{\circ}C.$

• Korean Chemical Engineering Research
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• v.45 no.6
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• pp.669-676
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• 2007

The raw water was fractionated into hydrophobic (HPO), transphilic (TPI), and hydrophilic portions (HPI) using XAD resins. The raw water DOC contains 39% of hydrophilics, 43% of hydrophobics, and 18% of transphilics. When fractionated NOM (natural organic matter) was passed through hydrophilic membrane with 100 kDa, hydrophobic portion (HPO) caused the most fouling and hydrophilic portion (HPI) caused the least fouling. This could be related to size and adsorption capability of organics. Small sized organics would pass through membrane pores, but large sized organics would be attracted to either membrane pores or surface, which led to the fouling. An effect of membrane pore size on membrane fouling is related to the availability of organics at membrane pores. As the pore size became larger, the more organics were transported into the membrane pore. Some organics caused pore blocking, and others caused pore adsorption, which resulted in membrane fouling. Membrane material is also important for membrane fouling. More fouling occurred at hydrophobic membrane than hydrophilic membrane regardless of its pore size. Hydrophobic interaction caused more fouling at hydrophobic membrane.

• Textile Coloration and Finishing
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• v.13 no.3
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• pp.172-179
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• 2001

In order to improve dye uptime and wash fastness on dyeing of cotton fabrics with Amur cork tree, twitter ionic groups, acid groups, hydrophobic groups or cross linkage were introduced into cotton fabrics. Results obtained were as follows, 1 The optimum modification of cotton fabrics was carbosy methylation in the water solution containing 15% sodium chloroacetate and 15% sodium hydroxide and then introducing hydrophobic groups by treating in the solution containing $30m\ell$ DMSO and $3m\ell$ 2,4-TDI 2. Numbers of carbon, diisocyanate group than monoisocyanate group and aromatic compound than aliphatic compound in introduced hydrophobic groups were effective. 3. The dye uptake and wash fastness wore enhanced significantly by treating only with 2,4-TDI. 4. The wash fastness seems to correlate to the degree of swelling of the fabric during washing and also depend on the Interaction between dyes and acid groups as well as hydrophobic groups.

• Bulletin of the Korean Chemical Society
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• v.31 no.2
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• pp.442-446
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• 2010

Adenosine 3',5'-cyclic monophosphate (cAMP) is a second messenger responsible for a multitude of cellular responses. In this study, we utilized $\beta$-cyclodextrin ($\beta$-CD) as an artificial receptor with a hydrophobic cavity to elucidate the inclusion kinetics of cAMP in a hydrophobic environment using the ultrasonic relaxation method. The results revealed that the interaction of cAMP with $\beta$-CD followed a single relaxation curve as a result of host-guest interactions. The inclusion of cAMP into the $\beta$-CD cavity was found to be a diffusion-controlled reaction. The dissociation of cAMP from the $\beta$-CD cavity was slower than that of adenosine 5'-monophosphate (AMP). The syn and anti glycosyl conformations of adenine nucleotides are considered to play an important role in formation of the inclusion complex. Taken together, our findings indicate that hydrophobic interactions are involved in the inclusion complex formation of cAMP with $\beta$-CD and provide insight into the interactions of cAMP with cAMP-binding proteins.