• Molecules and Cells
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• v.26 no.1
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• pp.61-66
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• 2008

Cyclic AMP receptor protein (CRP) is allosterically activated by cAMP and functions as a global transcription regulator in enteric bacteria. Structural information on CRP in the absence of cAMP (apo-CRP) is essential to fully understand its allosteric behavior. In this study we demonstrated interdomain interactions in apo-CRP, using a comparative thermodynamic approach to the intact protein and its isolated domains, which were prepared either by limited proteolysis or using recombinant DNA. Thermal denaturation of the intact apo-CRP, monitored by differential scanning calorimetry, revealed an apparently single cooperative transition with a slight asymmetry. Combined with circular dichroism and fluorescence analysis, the thermal denaturation of apo-CRP could be interpreted as a coupled process involving two individual transitions, each attributable to a structural domain. When isolated individually, both of the domains exhibited significantly altered thermal behavior, thus pointing to the existence of non-covalent interdomain interactions in the intact apo-CRP. These observations suggest that the allosteric conformational change of CRP upon binding to cAMP is achieved by perturbing or modifying pre-existing interdomain interactions. They also underline the effectiveness of a comparative approach using calorimetric and structural probes for studying the thermodynamics of a protein.

• Journal of Photoscience
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• v.9 no.2
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• pp.296-298
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• 2002

Irreversible photobleaching of bacteriorhodopsin (bR), namely denaturation induced by illumination of visible light, was investigated by absorption kinetic measurements. The denaturation kinetics revealed that light illumination significantly enhanced the structural decay of bR. The kinetic analyses showed that the molecular structure of bR denatures according to a single-exponential decay, whereas irreversible photobleaching has two decay components. The decay constant of the slow component of photobleaching is almost same as that in the dark. An Arrhenius plot of the denaturation kinetic constants for the fast and slow components showed similar activation energies of approximately 19 kcal/mol.

• Food Science of Animal Resources
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• v.20 no.2
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• pp.146-151
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• 2000

The objective of this study was to investigate the characteristics on the thermal denaturation of free drip released from pork loin during chilled storage using DSC(differential scanning calorimetry). DSC thermogram of drip released from normal pork(NORD) was characterized by a minor peak and two major peaks with temperature maxima at $61.5^{\circ}C$, $71.7^{\circ}C$ (associated with sarcoplasmic proteins) and $84.3^{\circ}C$ (associated with protein-protein interaction and aggregation). In the denaturation temperature of drip released from PSE pork (PSED), the peak(Tmax) at $59.0^{\circ}C$ was reduced by $2.5^{\circ}C$. When the thermograms were divided into segments correponding to the three peaks, $\Delta$H2 was shown to be reduced by 10% in PSED as compared to NORD. With the decrease in the solubility of sarcoplasmic proteins in PSE muscle, there was a corresponding increase the drip loss during the storage.

• Food Science of Animal Resources
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• v.18 no.4
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• pp.358-363
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• 1998

The objectives of this study were to evaluate the effect of previous heating temperature and holding times on the thermal behavior of pork loin muscle by DSC. Pork loin muscles were heated to achieve the following end-point temperatures: 40$^{\circ}C$, 50$^{\circ}C$, 60$^{\circ}C$, 70$^{\circ}C$, 80$^{\circ}C$ at heating rate = 10$^{\circ}C$/min. The first peak was disappeared when samples were initially heated to 50$^{\circ}C$ for 1 minute. As end-point temperature was raised, major peaks were progressively disappeared and peaks were lost completely at 80$^{\circ}C$. Especially, peaks were completely disappeared at 70$^{\circ}C$ for 10 minute. Increasing of exposure time to elevated temperature also increased denaturation, thereby reducing the area of the thermogram.

• Journal of the Korean Society of Radiology
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• v.9 no.7
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• pp.509-513
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• 2015

In this study, we evaluated the thermal denaturation characteristics of reusable NIPAM tissue mimicking (TM) Phantom by measuring the thermal sensitivity. And the changes of acoustic characteristic and thermal denaturation shape in NIPAM TM phantom according to the number of re-use time and re-use period were observed. With the result, as the sonication time is increased, the sound velocity of NIPAM phantom was decreased by 100 m/s and the attenuation was increased slightly. However, the changes according to the re-use period was not observed. In the thermal denaturation shape and size observation by ultrasound sonicaton, the remarkable changes have not been confirmed. With the result of this study, NIPAM Phantom was considered appropriate to evaluate and predict the effect of therapeutic ultrasound by in repeated sonication test.

• Food Science of Animal Resources
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• v.37 no.1
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• pp.44-51
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• 2017

Heat treatment of milk aims to inhibit the growth of microbes, extend the shelf-life of products and improve the quality of the products. Heat treatment also leads to denaturation of whey protein and the formation of whey protein-casein polymer, which has negative effects on milk product. Hence the milk heat treatment conditions should be controlled in milk processing. In this study, the denaturation degree of whey protein and the combination degree of whey protein and casein when undergoing heat treatment were also determined by using the Native-PAGE and SDS-PAGE analysis. The results showed that the denaturation degree of whey protein and the combination degree of whey protein with casein extended with the increase of the heat-treated temperature and time. The effects of the heat-treated temperature and heat-treated time on the denaturation degree of whey protein and on the combination degree of whey protein and casein were well described using the quadratic regression equation. The analysis strategy used in this study reveals an intuitive and effective measure of the denaturation degree of whey protein, and the changes of milk protein under different heat treatment conditions efficiently and accurately in the dairy industry. It can be of great significance for dairy product proteins following processing treatments applied for dairy product manufacturing.

• BMB Reports
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• v.35 no.5
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• pp.472-475
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• 2002

Phaseolus vulgaris phytohemagglutinin L is a homotetrameric-leucoagglutinating seed lectin. Its three-dimensional structure shows similarity with other members of the legume lectin family. The tetrameric form of this lectin is pH dependent. Gel filtration results showed that the protein exists in its dimeric state at pH 2.5 and as a tetramer at pH 7.2. Contrary to earlier reports on legume lectins that possess canonical dimers, thermal denaturation studies show that the refolding of phytohemagglutinin L at neutral pH is irreversible. Differential scanning calorimetry (DSC) was used to study the denaturation of this lectin as a function of pH that ranged from 2.0 to 3.0. The lectin was found to be extremely thermostable with a transition temperature around $82^{\circ}C$ and above $100^{\circ}C$ at pH 2.5 and 7.2, respectively. The ratio of calorimetric to vant Hoff enthalpy could not be calculated because of its irreversible-folding behavior. However, from the DSC data, it was discovered that the protein remains in its compact-folded state, even at pH 2.3, with the onset of denaturation occurring at $60^{\circ}C$.

• Proceedings of the Korean Society of Near Infrared Spectroscopy Conference
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• 2001.06a
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• pp.1628-1628
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• 2001

Near infrared (NIR) spectroscopy is a powerful technique for non-destructive analysis that can be obtained in a wide range of environments. Recently, NIR measurements have been utilized as probe for quantitative analysis in agricultural, industrial, and medical sciences. In addition, it is also possible to make practical application on NIR for molecular structural analysis. In this work, Fourier transform near infrared (FT-NIR) measurements were carried out to utilize extensively in the relative amounts of different secondary structures were employed, such as Iysozyme, concanavalin A, silk fibroin and so on. Several broad NIR bands due to the protein absorption were observed between 4000 and $5000\;^{-1}$. In order to obtain more structural information from these featureless bands, second derivative and Fourier-self-deconvolution procedures were performed. Significant band separation was observed near the feature at $4610\;^{-1}$ ,. Particularly the peak intensity at $4525\;^{-1}$ shows a characteristic change with thermal denaturation of fibroin. The structural information can be also obtained by mid-IR and CD spectral. Correlation of NIR spectra with protein structure is discussed.

• Korea-Australia Rheology Journal
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• v.19 no.2
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• pp.81-88
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• 2007

Blends of collagen dispersion (COL) with poly(vinyl alcohol) (PVA) in different weight ratios were investigated by oscillatory rheometry, Fourier transform-infrared spectroscopy and scanning electron microscopy. It was found that even with 80% of PVA, the COL/PVA blends behaved more like collagen dispersion than pure PVA solution in the dynamic thermal and frequency processing, for instance, a dominant elastic appearance (G'>G"), a similar shear thinning behavior and the thermal denaturation below $40^{\circ}C$. However, influence on the blend behaviour by PVA was noticeable, for instance, an increase of dynamic denaturation temperature, the decreasing intensity of amide I, II and III bands as well as the diminishing irregular pores on the surface of blends. The interaction between collagen and PVA could be observed, especially at the regions with low content or high content of PVA.

• Bulletin of the Korean Chemical Society
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• v.35 no.8
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• pp.2523-2528
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• 2014

In the present study, at first, azo Schiff base ligand of (N,N'-bis(5-phenylazosalicylaldehyde)-ethylenediamine) ($H_2L$) has been synthesized by condensation reaction of 5-phenylazosalicylaldehyde and ethylenediamine in 2:1 molar ratio, respectively. Then, its cobalt complex (CoL) was synthesized by reaction of $Co(OAc)_2{\cdot}4H_2O$ with ligand ($H_2L$) in 1:1 molar ratio in ethanol solvent. This ligand and its cobalt complex containing azo functional groups were characterized using elemental analysis, $^1H$-NMR, UV-vis and IR spectroscopies. Subsequently, the interaction between native calf thymus deoxyribonucleic acid (ct-DNA) and CoL complex was investigated in 10 mM Tris/HCl buffer solution, pH = 7 using UV-vis absorption, thermal denaturation technique and viscosity measurements. From spectrophotometric titration experiments, the binding constant of CoL complex with ct-DNA was found to be $(2.4{\pm}0.2){\times}10^4M^{-1}$. The thermodynamic parameters were calculated by van't Hoff equation.The enthalpy and entropy changes were $5753.94{\pm}172.66kcal/mol$ and $43.93{\pm}1.18cal/mol{\cdot}K$ at $25^{\circ}C$, respectively. Thermal denaturation experiments represent the increasing of melting temperature of ct-DNA (about $0.93^{\circ}C$) due to binding of CoL complex. The results indicate that the process is entropy-driven and suggest that hydrophobic interactions are the main driving force for the complex formation.